Abstract: Chlorine and calcium ions are measured in a biological sample using a maltose derivative having a chromogenic group at the reducing end. These ions are accurately measured in biological samples such as blood and urine without influence of amylase that may be present in such samples.

Abstract: The present invention provides a method for the pretreatment of object surfaces prior to taking a sample for microbial analysis. The method uses a blend to remove biofilms without hindering the growth of microorganisms. The method allows for reliable and replicable determination of microorganisms formed on the investigated surfaces.

Abstract: A stable, single liquid alpha-amylase assay reagent comprises a polysaccharide or long chain oligosaccharide substrate for alpha-amylase having an optically detectable label bonded to the reducing end glucose, by a bond cleavable by alpha- or beta-glucosidase, and a blocking group bonded to the terminal end glucose. The reagent further comprises beta-amylase and either alpha- or beta-glucosidase. Sorbitol is provided in an amount of about 5% to retard degradation of the enzymes. Zwitterionic buffers are also provided to stabilize the enzymes. In preparing the reagent, the enzymes and substrate are filtered through a 0.2 micron or less filter to remove alpha-amylase producing organisms.

Abstract: In accordance with a novel process, (R)-amines of the formula ##STR1## in which R.sup.1, R.sup.2 and n have the meanings given in the description, can be prepared by reacting reating N-acyl-amines of the formula ##STR2## in which R.sup.1, R.sup.2, R.sup.3 and n have the meanings given in the description,with lipases which are suitable for cleaving the (R)-enantiomers of N-acyl-amines of the formula (II), in the presence of water and optionally in the presence of an organic diluent, at a pH of between 3.0 and 10.0 and at temperatures of between 0.degree. C. and 80.degree. C.

Abstract: A method of inhibiting proteolytic degradation of a thermally-stable intracellular protein is described. The method involves adding 1 or more denaturing agents to a sample which contains the protease and the protein of interest and heating the resulting solution at a temperature and for period of time sufficient to denature the protease. The method optionally includes a step for lysing the cell if the protein of interest is contained in a cell in order to release said protein. Additionally, a method of determining Mx protein induced by interferon in a blood sample is described. The method involves adding to a blood sample a lysing agent, a denaturing agent, and a detergent selected to solubilize Mx protein. The sample containing Mx protein is then heated at a temperature of from about 50.degree. C. to about 60.degree. C. for a period of time of from about 1 minute to about 30 minutes, and the Mx protein in the solution then is determined.

Abstract: A bacteria impermeable container or ampule (10) contains a liquid growth medium and a substrate-indicator complex. The complex includes a substrate component, e.g., starch, and an indicator molecule, e.g., a dye, a fluorescent molecule, or the like, which are tightly bound and complexed, but which are cleavable by a preselected enzyme. A sterilant passes over a carrier (20) for microorganisms which, upon germination, are capable of rapidly generating large quantities of the preselected enzyme. Following the sterilization process, the carrier is immersed in the liquid growth medium. Any viable surviving microorganisms grow, generating the preselected enzyme. The enzymes cleave the bound indicator molecule from the substrate, resulting in a measurable property change in a couple of hours. Typical property changes include fluorescence, a color change, a change in pH which triggers a pH indicator color change, and the like.

Abstract: A method for increasing the accuracy of photometric-based assays for .alpha.-amylase by subjecting a sample to a secondary interrogating beam of radiation at a wavelength distinguishable from a primary interrogating beam of radiation. The secondary interrogating beam of radiation is indicative of an interfering reaction occurring in the absence of analyte at the primary wavelength. The secondary wavelength is outside the absorption spectrum of the analyte of interest. This secondary radiation beam's absorption is proportional to the interfering reaction at the primary wavelength.

Abstract: The use of amylopectin-type starch obtained from potato that has been modified by genetic engineering to suppress the formation of amylose-type starch as a filling agent in the preservation of food-stuff, is described.

Abstract: ABSTRACT OF THE DISCLOSURE A stable starch based adhesive with good adhesive properties at low solids and high viscosity is prepared by a two-step process wherein starch is first converted using acid or alpha-amylase followed by further conversion withbeta-amylase.

Abstract: The present invention relates to a peroxidase-containing reagent comprising a buffered aqueous solution of a peroxidase conjugate and a substrate for the peroxidase, in the absence of peroxide. The invention further relates to a method of stabilizing the peroxidase activity of a buffered aqueous solution containing a peroxidase conjugate. Further, the invention relates to a tetramethylbenzidine peroxidase substrate reagent and to a method of preparing same.

Abstract: An improved method for determining the presence of an analyte in an oral fluid sample. A portion of the sample is mixed or contacted with a chromogenic substrate effective to produce a colored product upon reaction with .alpha.-amylase present in the sample. After a selected reaction time, the reaction mixture is inspected to determine the level of such colored product produced. Production of a level of colored product above a selected threshold within the reaction time indicates that an effective volume of undiluted oral fluid sample has been collected which is sufficient to allow detection of the analyte. A device for use in the method is also disclosed.

Abstract: A process suitable for use in the sequencing of an oligosaccharide compound includes a first analysis of a primary oligosaccharide compound's monosaccharide composition, selection of sequencing agents to apply to the oligosaccharide compound, applying a selected sequencing agent to the oligosaccharide compound, and analyzing a released monosaccharide to select a second sequencing agent. The sequencing agent may be, for example, an enzyme. The oligosaccharide compound may be, for example, an oligosaccharide, or a product of an oligosaccharide, or a species having an oligosaccharide portion.

Abstract: Enzyme activity is measured promptly with a high accuracy by introducing an enzyme, the activity of which is to be measured, into a column comprising a hollow tube packed with a filler comprising a support and a substrate that can be recognized by the enzyme, which is immobilized on the support, and measuring the amount of the obtained decomposition product of the substrate.

Abstract: The invention concerns new indophenyl-substituted maltose derivatives, their use for the determination of the enzymatic activity of .alpha.-amylase and reagents for the determination of .alpha.-amylase which contain the new indophenyl-substituted maltose derivatives as the enzyme substrate.

Abstract: The present invention relates to stably co-transfected eukaryotic cell lines capable of expressing a recombinant GABA.sub.A receptor, particularly a recombinant human GABA.sub.A receptor, which comprises at least one alpha, one beta and one gamma subunit; and to the use of the cell line and/or membrane preparation in selecting compounds and designing medicaments which interact with the respective human recombinant GABA.sub.A receptor.

Abstract: A method for determining .alpha.-amylase activity which involves bringing a sample into contact with an .alpha.-glucosidase in the presence of an .alpha.-amylase substrate and optically determining a liberated label, the substrate being a maltooligosaccharide composed of at least 3 glucose units, whose reducing terminal glucose is bonded to an optically measurable label at the 1-position by .alpha.-glucoside linkage or .beta.-glucoside linkage, and whose non-reducing terminal glucose is modified by a substituent other than glucose, and the .alpha.-glucosidase being substantially capable of acting on glucose to which the label is bonded at the 1-position by .alpha.-glucoside linkage and on all maltooligosaccharides having 2 to 7 glucose units; and a reagent for determining .alpha.-amylase activity comprising the .alpha.-glucosidase and said .alpha.-amylase substrate. The present invention permits, in the determination of .alpha.

Abstract: The invention is a non-invasive diagnostic test which is performed on the surface of the skin. This test indicates skin cholesterol levels which can provide information about the extent of aortic atherosclerosis. The invention also relates to reagents in the form of affino-enzymatic test compounds for use in the diagnostic test.

Abstract: An immunoassay element for quantitatively analyzing a ligand by determining the change in enzymatic activity caused by a reaction between the ligand, a linked product of the ligand and a high molecular weight compound and an enzyme-labelled antibody. The immunoassay element comprises a substrate layer containing a non-diffusible substrate which forms a diffusible material in the presence of the enzyme, and a reagent layer containing a fragmenting enzyme for further fragmenting the non-difussible material. Also provided is a process for quantitatively analyzing a ligand contained in a sample by the use of the immunoassay element.

Abstract: An immunoassay element for quantitatively analyzing a ligand by determining the change in enzymatic activity. When the ligand is a low molecular weight antigen, competitive reactions between the ligand, enzyme-labelled antibody and conjugate of the antigen and high molecular weight compound are utilized. When the ligand is a macromolecular antigen, a reaction between the ligand and an enzyme-labelled antibody is utilized directly. The immunoassay element comprises a substrate layer containing a non-diffusible substrate which forms a diffusible material in the presence of the enzyme, and a reagent layer for detecting the thus formed diffusible material. The non-diffusible substrate is composed of a pulverized insoluble polysaccharide. The reagent layer may further contain a fragmenting enzyme for further fragmenting the non-diffusible material.

Abstract: Enzymatically clearable chemiluminescent 1,2-dioxetane compounds capable of producing light energy when decomposed, substantially stable at room temperature before a bond by which an enzymatically clearable labile substituent thereof is intentionally cleaved, are disclosed. These compounds can be represented by the formula: ##STR1## wherein: X and X.sup.1 each represent, individually, hydrogen, a hydroxyl group, a halo substituent, an unsubstituted lower alkyl group, a hydroxy (lower) alkyl group, a halo (lower) alkyl group, a phenyl group, a halophenyl group, an alkoxyphenyl group, a hydroxyalkoxy group, a cyano group or an amide group, with at least one of X and X.sup.1 being other than hydrogen; and R.sub.1 and R.sub.2, individually or together, represent an organic substituent that does not interfere with the production of light when the dioxetane compound is enzymatically cleaved and that satisfies the valence of the dioxetane compound's 4-carbon atom, with the provisos that if R.sub.1 and R.sub.

Abstract: A novel method of screening for novel secreted mammalian proteins is described in which mammalian secretory leader sequences are detected using the yeast invertase gene as a reporter system.

Abstract: A method and culture and detection medium for selectively detecting yeasts of the species Candida albicans involving placing a sample to be analyzed directly in contact with (1) a culture and detection medium containing a nutrient base metabolized by yeasts, (2) a chromogenic or fluorigenic substrate capable of being hydrolyzed by a hexosaminidase enzyme that is associated with Candida albicans, and (3) at least one hexosaminidase-containing compound capable of activating hexosaminidase enzymes. A kit for carrying out the method for selectively detecting yeasts of the species Candida albicans is also provided.

Abstract: The present invention provides an assay method for hemicellulases comprising a) directly dyeing, using a reactive dye, an insoluble natural product, or a modified form of a natural fibre material; and b) adding the enzyme to the dyed product produced in step a) and, after a specific incubation period, separating the liquid component from the insoluble dyed product, e.g. by a simple filtration, and determining the amount of dyestuff liberated in the the separated solution by spectrophotometric means. A combined mixing and dispensing device for use in the method of the present invention is also provided.

Abstract: A process for differentially determining .alpha.-amylase isoenzyme activities by the inhibitor method, in which 6.sup.3 -deoxymaltotriose (DOG3) represented by the formula ##STR1## is used as an inhibitor.

Abstract: A method is provided for determining glucose-6-phosphate, including the step of dehydrogenating glucose-6-phosphate and NAD or NADP in the presence of glucose-6-phosphate dehydrogenase to produce 6-phosphogluconate and NADH or NADPH, wherein the determination is carried out in the presence of 6-phosphogluconolactonase. Also provided is a composition for determining glucose-6-phosphate, characterized by containing 6-phosphogluconolactonase, glucose-6-phosphate dehydrogenase, and NAD or NADP.

Abstract: A composition for determination of chloride ion, comprising a maltooligosaccharide derivative possessing modified or non-modified non-reducing terminal and modified reducing terminal, a metal chelating agent, .alpha.-amylase and an adjuvant enzyme, provided that the adjuvant enzyme may not be contained when the maltooligosaccharide derivative possesses reducing terminal with a modifying group bound in .alpha.-type, which does not require maintenance and control of special instruments and special treatment of waste liquors, affords good analytic efficiency, determination precision and linearity, and is capable of suppressing rise of reagent blank and giving accurate determination values from test samples showing high values.

Abstract: A method for the estimation of a salicylate in a sample is characterized by enzymatically converting the salicylate to a catechol by the action of a salicylate mono-oxygenase enzyme on the salicylate in the presence of a reduced pyridine nucleotide, reacting the catechol with a compound selected from compounds of formula I or amine or phenolic compounds of formulae II, III or IV ##STR1##

Abstract: An enzyme-labelled antibody adapted for use in a homogeneous immunoassay is provided. The enzyme-labelled antibody is a conjugate of an enzyme with two or more different monoclonal antibodies, each of the monoclonal antibodies being capable of specifically recognizing and binding to a different epitope of the same antigen. By using the enzyme-labelled antibody in the homogeneous enzyme immunoassay process, an analyte can be quantitatively analyzed at a higher sensitivity through a simple operation. Also provided is a dry immunoassay element comprising an immunological reaction layer containing the enzyme-labelled antibody. By the provision of such an immunoassay element, a further simplified quick analysis of an analyte is realized to give an accurate result.

Abstract: Subject matter of the invention is a new method of detecting a substance with hydrolase activity in a sample, characterized in that the sample is brought into contact with an indicator enzyme, which is covalently bound to an insoluble carrier material and can be rendered soluble by the hydrolase activity, in that the cleaved off indicator is separated and in that its enzymatic activity is determined and test means for its implementation.

Abstract: A process and a reagent for the determination of ions in fluids, wherein the influence of these ions on the activity of an enzyme is measured. The ions for example are sodium, potassium, calcium, magnesium, manganese, lithium, lead, zinc, copper, iron or other heavy metals or non-metallic ions comprising chloride, bicarbonate, protons, ammonium and substances that give rise to ammonium. The enzymes which are used may be a transferase, a hydrolase, an oxidoreductase or a lyase. An essential feature is a method to exclude interferences by ions by masking the interfering ions with a binding agent.

Abstract: A method is provided, in one embodiment, for the determination of an analyte in a biological fluid sample in the presence of a substance interfering with an assay for the analyte. This embodiment is implemented by using antibodies to cause the selective immunoreaction of at least one of the analyte or the interfering substance and then conducting an assay for the analyte in at least one of the immunoreactants or the non-reactants. Another embodiment provides a disposable reaction device to implement the method. The invention is applicable to the detection of a wide variety of analytes, including cholesterol in a targeted lipoprotein class in the presence of cholesterol in another class; to targeted isozymes of enzymes such as creatine kinase, lactate dehydrogenase, amylase, and alkaline or acid phosphatases in the presence of other isozymes; as well as to targeted immunoglobulins in the presence of non-targeted immunoglobulins.

Abstract: A polyacyl maltooligosaccharide derivative which is a precursor of a maltooligosaccharide derivative having modified groups at the 6-position or 4- and 6-positions of non-reducing end glucose unit and being effectively used as a substrate for measuring .alpha.-amylase activity, can be produced under mild conditions by crosslinking OH groups in the non-reducing end glucose unit of oligosaccharide with a benzylidene group having an alkoxy group, followed by acylation and treatment with a dilute acid.

Abstract: A reagent for determining a-amylase activity, comprising a maltooligosaccharide derivative of the following formula ##STR1## (wherein either one of R.sub.1 and R.sub.2 is .beta.-galactopyranosil and the other is hydrogen, R.sub.3 is a group bonded to the reducing terminal glucose via a bond cleavable by .alpha.-amylase, which becomes a measurable substance upon cleavage of the bond, and n is an integer of 0-2), which does not comprise adjuvant enzymes; and a method for determining .alpha.-amylase activity which comprises use of the reagent. The reagent of the present invention does not require use of any adjuvant enzyme and is stable since the substrate is not exposed to the decomposition by an adjuvant enzyme. The substrate used in the present invention has high affinity for .alpha.-amylase. Thus, the reagent and the determination method of the present invention make it possible to determine .alpha.-amylase activity with high sensitivity.

Abstract: In a single liquid alpha-amylase reagent composition comprising an aqueous solution of at least one substrate which is hydrolyzed when mixed with a sample of body fluid containing alpha-amylase to yield a detectable label, alpha-glucosidase from Bacillus stearothermophilus is used to cooperate with the alpha-amylase in the formation of the detectable label and the composition being stable against degradation for a least 6 months at 2.degree. to 10.degree. C.

Abstract: A process and a reagent for the determination of ions in fluids, wherein the influence of these ions on the activity of an enzyme is measured. The ions for example are sodium, potassium, calcium, magnesium, manganese, lithium, lead, zinc, copper, iron or other heavy metals or non-metallic ions comprising chloride, bicarbonate, protons, ammonium and substances that give rise to ammonium. The enzymes which are used may be a transferase, a hydrolase, an oxidoreductase or a lyase. An essential feature is a method to exclude interferences by ions by masking the interfering ions with a binding agent.

Abstract: A process and a reagent for the determination of ions in fluids, wherein the influence of these ions on the activity of an enzyme is measured. The ions for example are sodium, potassium, calcium, magnesium, manganese, lithium, lead, zinc, copper, iron or other heavy metals or non-metallic ions comprising chloride, bicarbonate, protons, ammonium and substances that give rise to ammonium. The enzymes which are used may be a transferase, a hydrolase, an oxidoreductase or a lyase. An essential feature is a method to exclude interferences by ions by masking the interfering ions with a binding agent.

Abstract: A process and a reagent for the determination of ions in fluids, wherein the influence of these ions on the activity of an enzyme is measured. The ions for example are sodium, potassium, calcium, magnesium, manganese, lithium, lead, zinc, copper, iron or other heavy metals or non-metallic ions comprising chloride, bicarbonate, protons, ammonium and substances that give rise to ammonium. The enzymes which are used may be a transferase, a hydrolase, an oxidoreductase or a lyase. An essential feature is a method to exclude interferences by ions by masking the interfering ions with a binding agent.

Abstract: The subject invention provides a method for analyzing the metabolic activity in cells by improving the retention of a detectable reporter molecule only in intact cells where a particular enzyme is present. In particular, improved retention results from a two part process involving conjugation of haloalkyl-substituted derivatives of a reporter molecule with intracellular cysteine-containing peptides while unblocking the reporter molecule. The method for analyzing metabolic activity of cells involves the use of a substrate having the formXR-REPORTER-BLOCKwherein -BLOCK is a group selected to be removable by action of a specific analyte, to give REPORTER spectral properties different from those of the substrate,-REPORTER- is a molecule that, when no longer bound to BLOCK by a BLOCK-REPORTER bond, has spectral properities different from those of the substrate, andXR-- is a haloalkyl moiety that can covalently react with an intracellular thiol (Z--S--H) to form a thioether conjugate (Z--S--R--).

Abstract: Differential assay of human pancreatic .alpha.-amylase and human salivary .alpha.-amylase can be made extremely easily with good accuracy using a reducing-end modified maltooligosaccharide derivative as a substrate, by acting coupled enzymes having different substrate specificities on the degradation products formed by the hydrolytic action of .alpha.-amylases and measuring the resulting reaction products.

Abstract: An aromatic substituted glycoside is disclosed of the formula ##STR1## wherein the configuration of the substituted --OR on the anomeric carbon is alpha, n is an integer of 0 or 1, and R is a substituted aromatic radical selected from the group ##STR2## where R.sub.1 through R.sub.6 are independently halogen, NO.sub.2, SO.sub.3 H, COR.sub.7, ##STR3## where R.sub.7 is lower alkyl; and includes its stereoisomers, optical isomers and geometric isomers and mixtures of the foregoing isomers. These substrates are useful as direct substrates for alpha-amylases. A process for the preparation of the substrates and related substances is also described.

Abstract: .alpha.-Amylase activity can be determined rapidly and precisely by using as a substrate a modified oligo-saccharide wherein a benzylozymethyl group or a halo-methyl group is bonded to the C.sub.6 position of non-reducing-end glucose residue and the reducing-end glucose residue is bonded to a group which exhibits an optically measurable change upon cleavage. Processes for producing such a compound are also disclosed.

Abstract: The present invention provides a process for the determination of an enzyme from an isoenzyme mixture in a liquid sample by inhibition of the disturbing isoenzymes and determination of the non-inhibited enzyme, wherein the isoenzyme mixture is contacted with one or more substances which are able to inhibit the disturbing isoenzymes, the sample containing the inhibiting substance(s) is transferred to a small-pored reaction medium and the disturbing enzyme is there inhibited and the determination of the non-inhibited enzyme is carried out in the resulting liquid.The present invention also provides a test carrier for carrying out this process.

Abstract: The present invention provides a maltooligoside derivative represented by the formula: ##STR1## wherein n denotes an integer 3-5, R represents an aromatic chromophoric group, X represents a group >CHCH.sub.2 N.sub.3 or >C.dbd.CH.sub.2, and Y represents a hydrogen atom, a substituted or unsubstituted hydrocarbon group or an alkyl- or arylsulfonyl group, a reagent for determining .alpha.-amylase activity which comprises said maltooligoside derivative as an effective ingredient, and a process for determining .alpha.-amylase activity, characterized in that said maltooligoside derivative and coupled enzymes are added to an .alpha.-amylase containing sample to conduct an enzymatic reaction and a liberated aromatic chromophoric compound is quantitatively determined. The compound of the present invention is very useful as a substrate for determining .alpha.-amylase activity, and .alpha.

Abstract: A maltooligosaccharide derivative very useful, for example, as a precursor of a modified oligosaccharide derivative having one or more modifying groups at the 6-position or the 4- and 6-positions of the non-reducing end glucose residue which can be effectively used as a substrate for determining .alpha.-amylase activity or an intermediate thereof, can be produced by reacting a compound of the formula: ##STR1## with a compound of the formula: ##STR2## to convert at least the hydroxyl groups at the 4- and 6-positions of non-reducing end glucose residue of the compound of the formula (1) into a cyclic boric acid ester, acylating the reaction product, and then treating the acylated product.

Abstract: The present invention provides a process for the specific determination of pancreatic .alpha.-amylase in the presence of salivary .alpha.-amylase in body fluids by reaction with a system for the detection of .alpha.-amylase with the use of an inhibitor for salivary .alpha.-amylase, wherein, as substrate, there is used a compound of the general formula: ##STR1## in which R.sub.1 is a straight-chained or branched alkyl or alkoyl radical containing up to 6 carbon atoms, a cycloalkyl or cycloalkoxyl radical containing 3 to 6 carbon atoms or a benzoyl, benzyl or phenyl radical which is optionally hydrophilically substituted, R.sub.2 is a hydrogen atom or in which R.sub.1 and R.sub.2 together form a methylene bridge, the hydrogen atoms of which, independently of one another, can each be substituted by an alkyl radical containing up to 5 carbon atoms or a phenyl radical, Gluc is a glucose molecule, n is 1, 2 or 3 and X is an optically determinable residue.

Abstract: A method and apparatus for the determination of the average molecular weight, average chain length or dextrose equivalent of starch and related carbohydrates containing glucose units. The starch is analyzed by determining the free glucose amount (Gf) contained in starch or related carbohydrate sample, determining a gross glucose amount (Gt) rendered by hydrolysis of starch or related carbohydrates, and further determining a glucose amount (Gr) rendered by hydrolysis of a reduced product which is obtained by reduction of reducing terminals contained in starch or related carbohydrate.The average molecular weight, average chain length or dextrose equivalent of the starch is determined using the formulas stated below from the measured amounts of the free glucose amount (Gf), and the glucose amount (Gr).

Abstract: Quantitative assay and reagent for the determination of chlorine ion in body fluid. Body fluid is contacted with a reagent which includes deactivated .alpha.-amylase, a compound capable of chelating calcium ion, a calcium chelate compound, and an .alpha.-amylase activity-measuring substance; the amount of .alpha.-amylase activity is proportional to the amount of chlorine ion present in the body fluid. The assay is suitable for automation.

Abstract: .alpha.-Amylase activity can be determined rapidly and precisely by using as a substrate a modified oligosaccharide wherein a benzyloxymethyl group or a halomethyl group is bonded to the C.sub.6 position of non-reducing-end glucose residue and the reducing-end glucose residue is bonded to a group which exhibits an optically measurable change upon cleavage. Processes for producing such a compound are also disclosed.

Abstract: Chromogenic enzyme substrate compounds comprising a dibenz[b,e] [1,4]oxazepinone or dibenzo[b,e] [1,4]thiazepinone nucleus having an enzyme-cleavable group such as a radical of a sugar, carboxylic acid, amino acid, peptide, phosphoric acid, or sulfuric acid. The substrate compounds are, in general, highly soluble in aqueous media and only slightly colored, and produce, upon enzyme cleavage, a chromogen exhibiting a large change in absorbance and a pKa below 7. Such substrates find use as indicators for the determination of enzyme analytes and enzymes used as markers in a variety of assays, including immunoassays.

Abstract: A method of oligosaccharide sequencing in which the components are determined essentially simultaneously is disclosed which comprises a series of steps as follows:A. Placing an identifying label on the reducing terminal residue of the oligosaccharide to be sequenced,B. Dividing said oligosaccharide into a plurality of separate portions of known integer amounts,C. Treating each said portion with a different reagent mix to thereby provide a series of reaction mixtures,D. Pooling known integer amounts of the products from each separate reaction mixture to give a product pool,E. Performing an analysis on said product pool which measures the molar proportions of the reaction products, andF. Reconstructing or identifying the starting oligosaccharide from the molar prevalence of said reaction products.