Abstract: This invention is directed to compositions and methods for determining target analytes. The compositions disclosed relate to cell-linker-probe complexes. The disclosed methods (including multiplex methods) utilize said cell-linker-probe complexes for target analyte determination.

Abstract: This invention pertains to methods, kits and compositions suitable for the detection, identification and/or quantitation of nucleic acids which are electrostatically immobilized to matrices using non-nucleotide probes which sequence specifically hybridize to one or more target sequences of the nucleic acid but do not otherwise substantially interact with the matrix. Once the nucleic acid is immobilized, the detectable non-nucleotide probe/target sequence complex, formed before or after the immobilization of the nucleic acid, can be detected, identified or quantitated under a wide range of assay conditions as a means to detect, identify or quantitate the target sequence in the sample. Because it is reversibly bound, the non-nucleotide probe/target sequence can optionally be removed from the matrix for detecting, identifying or quantitating the target sequence in the sample.

Abstract: This invention pertains to methods, kits and compositions suitable for the detection, identification and/or quantitation of nucleic acids which are electrostatically immobilized to matrices using non-nucleotide probes which sequence specifically hybridize to one or more target sequences of the nucleic acid but do not otherwise substantially interact with the matrix. Once the nucleic acid is immobilized, the detectable non-nucleotide probe/target sequence complex, formed before or after the immobilization of the nucleic acid, can be detected, identified or quantitated under a wide range of assay conditions as a means to detect, identify or quantitate the target sequence in the sample. Because it is reversibly bound, the non-nucleotide probe/target sequence can optionally be removed from the matrix for detecting, identifying or quantitating the target sequence in the sample.

Abstract: This invention pertains to methods, kits and compositions suitable for the detection, identification and/or quantitation of nucleic acids which are electrostatically immobilized to matrices using non-nucleotide probes which sequence specifically hybridize to one or more target sequences of the nucleic acid but do not otherwise substantially interact with the matrix. Once the nucleic acid is immobilized, the detectable non-nucleotide probe/target sequence complex, formed before or after the immobilization of the nucleic acid, can be detected, identified or quantitated under a wide range of assay conditions as a means to detect, identify or quantitate the target sequence in the sample. Because it is reversibly bound, the non-nucleotide probe/target sequence can optionally be removed from the matrix for detecting, identifying or quantitating the target sequence in the sample.

Abstract: This invention pertains to methods, kits and compositions suitable for the detection, identification and/or quantitation of nucleic acids which are electrostatically immobilized to matrices using non-nucleotide probes which sequence specifically hybridize to one or more target sequences of the nucleic acid but do not otherwise substantially interact with the matrix. Once the nucleic acid is immobilized, the detectable non-nucleotide probe/target sequence complex, formed before or after the immobilization of the nucleic acid, can be detected, identified or quantitated under a wide range of assay conditions as a means to detect, identify or quantitate the target sequence in the sample. Because it is reversibly bound, the non-nucleotide probe/target sequence can optionally be removed from the matrix for detecting, identifying or quantitating the target sequence in the sample.

Abstract: A peptide having the formulaA--Bwherein A represents an N-terminal protected amino acid residue or an optionally N-terminal protected peptide residue and B represents an optionally C-terminal protected amino acid residue, is prepared by reacting a substrate component selected from the group consisting of optionally N-terminal protected peptides of the formulaA--Xwherein A is as defined above and X represents an amino acidwith an amine component selected from the group consisting of(a) amino acids of the formulaH--B--OH,(b) optionally N-substituted amino acid amides of the formulaH--B--NHR.sup.3wherein B is an amino acid residue and R.sup.3 represents hydrogen, hydroxy, amino or alkyl, aryl or aralkyl, and(c) amino acid esters of the formula H--B--OR.sup.4 or H--B--SR.sup.4 wherein B is an amino acid residue and R.sup.4 represents alkyl, aryl and aralkyl,in the presence of a carboxypeptidase enzyme in an aqueous solution or dispersion having a pH from 5 to 10.5, preferably at a temperature of from 30 to 50.

Abstract: The B-30 amino acid in insulins is replaced enzymatically byreacting as substrate component the selected insulin Ins-X, wherein X represents the B-30 amino acidwith an amine component selected from the group consisting of(a) amino acids of the formulaH--B--OHwherein B is an amino acid residue,(b) optionally N-substituted amino acid amides of the formulaH--B--NR.sup.1 R.sup.2wherein B is an amino acid residue and R.sup.1 and R.sup.2 are independently selected from the group consisting of hydrogen, amino, hydroxy, alkyl, cycloalkyl, aryl, heteroaryl and aralkyl or R.sup.1 and R.sup.2 together with the nitrogen atom form a heterocyclic group which may contain a further hetero atom, and(c) amino acid esters of the formulaH--B--OR.sup.3, H--B--SR.sup.3 or H--B--SeR.sup.3wherein B is am amino acid residue and R.sup.

Abstract: An insulin such as porcine insulin is reacted enzymatically with an L-amino acid, amide, or ester in the presence of L-specific serine carboxypeptidase modified by reaction with divalent metal ions in aqueous solution or dispersion containing F.sup.-, Cl.sup.-, Br.sup.-, I.sup.-, CN.sup.-, or SCN.sup.-.

Abstract: Cu,Zn-superoxide dismutase (SOD) is isolated from aqueous solutions containing said enzyme together with accompanying proteins by chromatography of the solution at a pH of 4.7 to 5.0 on a cation exchange resin of the same polarity as SOD in the pH range used. As cation exchange resin may particularly be used carboxymethyl celluloses, cross-linked dextrans substituted with carboxymethyl groups or sulfopropyl groups or cross-linked agaroses substituted with carboxymethyl groups.The process lends itself to use on an industrial scale and provides a high yield of pure SOD.

Abstract: Cu,Zn-superoxide dismutase (SOD) is isolated from aqueous solutions containing said enzyme together with accompanying proteins by chromatography of the solution at a pH of 4.7 to 5.5 on a cation exchange resin of the same polarity as SOD in the pH range used. As cation exchange resin may particularly be used carboxymethyl celluloses, cross-liked dextrans substituted with carboxymethyl groups or sulfopropyl groups or cross-linked agaroses substituted with carboxymethyl groups.The process lends itself to use on an industrial scale and provides a high yield of pure SOD.

Abstract: Various enzymes, in particular Cu,Zn-superoxide dismutase (SOD), catalase and carbonic acid anhydrase, are recovered from blood by admixing wholly or partly isolated blood cells with ethanol or a homologous alcohol until a concentration of 10 to 70% by volume and allowing them to stand for hemolysis of the blood cells and denaturation of the hemoglobin, and then adding water up to the double volume or more, and removing the precipitate of cell residuals, hemoglobin and other denatured proteins from the suspension. Then the desired enzymes are isolated from the solution obtained.In particular, SOD and catalase can both be isolated by chromatography of the solution at a pH of 4.7 to 5.5 on a cation exchange resin of the same polarity as SOD in the pH range used and elution of the resin with a buffer solution which has a pH in the range 4.7 to 7.5 and an ionic strength in the range 0.01 to 1.0 M, SOD being eluted at the lowest pH and/or the lowest ionic strength.

Abstract: Cu,Zn-superoxide dismutase is recovered from yeast by plasmolysis with a small amount of ether or any other water immiscible, organic solvent and subsequent autolysis in water at a temperature of 25.degree. to 50.degree. C. and pH 5 to 9, following which the precipitate is removed and the superoxide dismutase is purified and isolated from the residual liquid, in particular by chromatography on carboxymethyl cellulose at pH 4.7 to 5.5.Cu,Zn-superoxide dismutase from Saccharomyces cerevisiae has the amino acid sequence: ##STR1## where Cys-57 and Cys-146 form a disulfide bond.

Abstract: A peptide having the formulaA--Bwherein A represents an N-terminal protected amino acid residue or an optionally N-terminal protected peptide residue and B represents an optionally C-terminal protected amino acid residue, is prepared byreacting a substrate component selected from the group consisting of(a) amino acid esters, peptide esters and depsipeptides of the formulaA--OR.sup.1 or A--SR.sup.1wherein A is as defined above and R.sup.1 represents alkyl, aryl, aralkyl or an .alpha.-des-amino fragment of an amino acid residue,(b) optionally N-substituted amino acid amides and peptide amides of the formulaA--NHR.sup.2wherein A is as defined above and R.sup.2 represents hydrogen, alkyl, aryl or aralkyl, and(c) optionally N-terminal protected peptides of the formulaA--Xwherein A is as defined above and X represents an amino acidwith an amine component selected from the group consisting of(a) amino acids of the formulaH--B--OH,(b) optionally N-substituted amino acid amides of the formulaH--B--NHR.sup.