Abstract: The present invention relates to the preparation of a novel heat-labile phosphatase enzyme from the filamentous fungus Aspergillus niger. This A. Niger phosphatase enzyme has a native molecular weight of approximately 80,000 daltons, and is shown by polyacrylamide gel electrophoresis under denaturing conditions to be an alpha-2 dimer consisting of identical subunits of molecular weight of approximately 37,000 daltons each. The native intact enzyme molecule has an isoelectric point (pI) of 4.6, and exhibits optimal functional activity under reaction conditions of neutral to slightly alkaline pH conditions (about pH 7.0 to about pH 8.5). This enzyme has two characteristics which make it valuable in molecular biology laboratory protocols. First, the enzyme is readily inactivated by mild heating conditions (50.degree. C.); and second, the enzyme is highly specific for DNA as a substrate for the hydrolysis reaction; it does not hydrolyze adenosine triphosphate (ATP).

Abstract: Xylanase is prepared by cultivation of a fungus in a nutrient medium which contains corn cobs. The fungus is preferably Thermomyces lanuginosus DSM 5826 which produces an exo- and endo- cellulase-free xylanase.

Abstract: A method for the production of human tissue type plasminogen activator (human t-PA) using cells is disclosed. The method comprises producing the human t-PA in parallel with the growth of the cells or after the cells have been grown. To the cell culture bicarbonate ion is added at a concentration equivalent to 3 to 10 g/l of NaHCO.sub.3 based on the true volume of the medium to increase the osmotic pressure of the medium to a range of 350 to 520 milliosmoles/liter.

Abstract: A process for the prodution of phosphatiolic acid is carried out by treating phospholipids with an enzyme capable of hydrolyzing a phospholipid into phosphatidic acid and a nitrogen-containing base and another enzyme capable of hydrolyzing a phospholipid into a diglyceride and a phosphoryl base. Further, another process for the production of phosphatidic acid is carried out by treating phospholipids with a treatment product of an oilseed is disclosed.

Abstract: Disclosed is a purified luciferase and a method for making it. The luciferase is obtained from Luciola cruciata. The luciferase has a pH range for stabililty of 6.5-9.0 and a optimum pH range of 8.0-9.5. The enzyme does not act on ADP, CTP, UTP and GTP.

Abstract: Novel bifunctional hydroxyphenylazobenzoic acid analogues (HABA-type and conjugates) and biotin analogues probiotin-type conjugates) useful as reagents in assays employing catalyzed reporter deposition are described as well as intermediates useful in synthesizing these compounds.

Abstract: An ascorbate oxidase having an optimum pH range of 3.5-4.5 is isolated from Acremonium sp. Hi-25 BP-3124. The ascorbate oxidase is used in foods or drinks to oxidize ascorbate to prevent damage to the foods or drinks by oxidation.

Abstract: An onco-developmentally regulated .alpha.-N-acetylgalactosaminyltransferase is isolated as a component of a particulate membrane fraction separated from cell and tissue homogenates which has the following characeristics:(a) Activity in Various Cells and Tissues--present in human fetal lung fibroblasts, hepatoma tissues and placenta, but absent from normal adult liver, lung, kidney and spleen tissues;(b) Substrate Specificity--acts on polypeptides comprising a sequence of val-thr-his-pro-gly-tyr by catalyzing .alpha.-N-acetylgalactosaminylation at the thr residue of the sequence;(c) Requirements for Metal Ion--requires metal ion for activity in 25 mM tris buffer, pH 7.6;(d) Optimal pH--optimal pH is about 7.6 asssayed in hepatoma cell homogenate in tris buffer and at a pH of about 6 to about 7 assayed in hepatoma cell homogenate enzyme activity is higher in 2(N-morpholino)ethanelsulfonic acid than in cacodylate buffer; and(e) Km--apparent Km for UDP - GalNAc is about 48 .mu.m.

Abstract: A new class of L-carnitine dehydrogenase is disclosed, which is stable in solution and has a residual activity of greater than 70% after one week in a pH 9.0 buffer solution at 5.degree. C., a molecular weight of 51,000.+-.6,000 daltons, a pH optimum of 9.0, a optimum temperature of 50.degree. C. and an isoelectric point of pH 5.3.+-.0.6. Also disclosed is a process for producing the new enzyme from a microorganism of the Alcaligenes genus, preferably the newly-discovered species Alcaligenes sp. No. 981 FERM BP-2570.

Abstract: A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:a) R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2b) R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.- carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: A method for making a stable aqueous liquid formulation containing at least one enzyme having proteolytic activity is disclosed. The method involves precipitating the enzyme from an aqueous medium with a salt to form a dispersion of the enzyme. The dispersion has a density of 1.22 g/cm.sup.3 to 1.23 g/cm.sup.3 due to the use of the salt. This process yields a sedimentation-resistant stable enzyme dispersion.

Abstract: A chorionic peptidase-1 (C-ase-1) which is isolThe U.S. government may have rights concerning the present invention because relevant developmental work was supported by NIH grant No. HD 14842.

Abstract: A thermostable lipase is produced by aerobically culturing a microorganism having the identifying characteristics of Bacillus sp.A30-1 ATCC No. 53841 on a nutrient medium under growth conditions until a recoverable lipolytic activity is detectable and thereafter isolating the thermostable lipase. The thermostable lipase has an optimum temperature of about 60.degree. C. and an optimum pH of about 9.5.

Abstract: Labelled triglyceride oils are produced for use in diagnostic breath tests. The process involves the cultivation of microorganisms capable of producing the oils in an appropriately controlled environment wherein the microorganisms are fed .sup.12 C or .sup.14 C labeled carbon substrates to induce the microorganisms to produce the labeled oils. The preferred labelled carbon substrate is a substrate containing .sup.12 C. The oil produced is preferrably enriched in oleic acid. The microorganisms can be induced to produce the oil by nitrogen depletion during cultivation.

Abstract: Amine-enriched proteins, having an increased isoelectric point are provided by reacting a naturally occurring protein with an amide bond forming agent in the presence of a polyamine or a salt thereof. Such amine-enriched proteins such as enzymes are useful as labels in immunoassays.

Abstract: A new transaminase has been isolated from E. coli DH-1 (ATCC 33849). It is possible to use the transaminase with great efficiency to prepare L-phosphinothricin and gamma-aminobutyric acid from appropriate precursors by transferring an amino group from glutamate.

Abstract: An isolated L-carnitine dehydrogenase is disclosed, which is stable in solution and has a residual activity of greater than 70% after one week in a pH 9.0 buffer solution at 5.degree. C. Also disclosed is a process for producing the new enzyme from a microorganism of the Alcaligenes genus, preferably the newly-discovered species Alcaligenes sp. No. 981 FERM BP-2570.

Abstract: Disclosed is a method of inhibiting phosphotyrosine phosphatase activity on a substrate which comprises preincubating the substrate with a pervanadate-containing solution. Also disclosed is the use of a solution comprising pervanate as an inhibitor of phosphotyrosine phosphatases and as a regulator of cell growth.

Abstract: A liquid thrombin preparation is prepared by reacting a unit of prothrombin with less than 5 units of thromboplastin in the presence of calcium, contacting the resultant thrombin with a phosphate buffer, and diluting and filtering the suspension. The filtrate is then applied sequentially to an anion-exchange agarose column and a cation-exchange agarose column and the thrombin fraction is step-wise eluted from the latter column with phosphate buffered saline. Liquid thrombin preparations thereby obtained have specific activities greater than 1,600 U/mg and can be used in haemostasis.

Abstract: A method for the production of human tissue type plasminogen activator (tPa) using cells is disclosed. The method includes a supplementation of a p-aminomethyl benzoic acid derivative to a cell culture medium or a tPA producing medium and further an increase of osmotic pressure in the medium to 350 milliosmoles or more/liter. The invention provides a method for producing single-chain tPA in a high concentration and with a relatively small amount of double-chain tPA in the medium.