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5449661 Angiotensin converting enzyme inhibitor and method for preparing same
PATENT ABSTRACTS
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5449615
AMPLIFICATION ASSAY FOR HYDROLASE ENZYMES
KDN-CLEAVING SIALIDASE ISOLATED FROM HEPATOPANCREAS OF MOLLUSKS
Rabin Brian R; Harbron Stuart; Eggelte Hendrikus J; Hollaway Michael R; Holloway legal representative Ann Potters Bar, UNITED KINGDOM assigned to London Biotechnology Limited Hydrolase enzymes are sensitively determined using novel substituted FAD substrates. The substituted FAD substrates are hydrolysed to FAD by the enzyme to be detected. The FAD is then combined with an apoenzyme to form a holoenzyme which is used to initiate a reaction that leads to a detectable product. When the hydrolase to be detected is phosphatase, the novel substrate is a phosphorylated derivative of FAD. A suitable apoenzyme is apo-glucose oxidase which provides exceptional sensitivity. Apo-D-amino acid oxidase, which is suitable for use in a single pot assay system, can also be used.
5449613 REACTING AN ENZYME IN A NON-AQUEOUS SOLVENT BY ADDING A LYOPHILIZATE OF ENZYME AND SALT TO THE SOLVENT Dordick Jonathan S; Khmelnitsky Yuri; Clark Douglas S Iowa City, IA, UNITED STATES assigned to The University of Iowa Research Foundation A method for reacting an enzyme in a non-aqueous organic solvent is disclosed. The method comprises preparing a lyophilizate of a salt which activates the enzyme and an enzyme wherein the lyophilizate contains a weight ratio of salt to enzyme of at least 60% salt sufficient to activate the enzyme in an organic solvent. The method then calls for dispersion of the lyophilizate in a non-aqueous organic solvent in the presence o f a substrate for the enzyme.
Li Yuh~eh; Li Su-Chen UNITED STATES
Metairie, LA,
A sialidase capable of cleaving a glycoconjugate to yield 3-deoxy-D-glycero-D-galacto2-nonulosonic acid (KDN) is isolated from hepatopancreas of mollusks. Preferably, the sialidase is isolated by processing crude oyster hepatopancreas to form a crude extract of the sialidase enzyme. The crude enzyme is further concentrated and refined utilizing sequential column chromatography fractogel EMD DEAE-650 (M), sephacryl S-200, and fractogel EMD SP 650 (M) chromatography, respectively. Using this procedure, the sialidase is purified over 155 fold with a 17% recovery. Ferric ion exerts a three fold stimulation in the activity of the sialidase, at a concentration of 3 mM. The sialidase cleaves 4-methylumbelliferyl-KDN, KDN alpha2 right arrow3Gal betal right arrow4GlcCer, KDN alpha2 right arrow6Gal betal right arrow4GlcCer, or KDN alpha2 right arrow6GalNAc-ol to yield KDN.
5449661 ANGIOTENSIN CONVERTING ENZYME INHIBITOR AND METHOD FOR PREPARING SAME Nakamura Yasunor; Takano Toshiaki Yokohama, JAPAN assigned to The Calpis Food Industry Co Ltd An angiotensin converting enzyme inhibitor contains as an effective constituent VaI-Pro-Pro and contains 3 to 10 amino acid residues. A method for producing the aforementioned angiotensin converting enzyme inhibitor involves fermenting a foodstuff material containing VaI-Pro-Pro as a constituent component with lactic acid bacteria.
563
5445942
5449615
AMPLIFICATION ASSAY FOR HYDROLASE ENZYMES
KDN-CLEAVING SIALIDASE ISOLATED FROM HEPATOPANCREAS OF MOLLUSKS
Rabin Brian R; Harbron Stuart; Eggelte Hendrikus J; Hollaway Michael R; Holloway legal representative Ann Potters Bar, UNITED KINGDOM assigned to London Biotechnology Limited Hydrolase enzymes are sensitively determined using novel substituted FAD substrates. The substituted FAD substrates are hydrolysed to FAD by the enzyme to be detected. The FAD is then combined with an apoenzyme to form a holoenzyme which is used to initiate a reaction that leads to a detectable product. When the hydrolase to be detected is phosphatase, the novel substrate is a phosphorylated derivative of FAD. A suitable apoenzyme is apo-glucose oxidase which provides exceptional sensitivity. Apo-D-amino acid oxidase, which is suitable for use in a single pot assay system, can also be used.
5449613 REACTING AN ENZYME IN A NON-AQUEOUS SOLVENT BY ADDING A LYOPHILIZATE OF ENZYME AND SALT TO THE SOLVENT Dordick Jonathan S; Khmelnitsky Yuri; Clark Douglas S Iowa City, IA, UNITED STATES assigned to The University of Iowa Research Foundation A method for reacting an enzyme in a non-aqueous organic solvent is disclosed. The method comprises preparing a lyophilizate of a salt which activates the enzyme and an enzyme wherein the lyophilizate contains a weight ratio of salt to enzyme of at least 60% salt sufficient to activate the enzyme in an organic solvent. The method then calls for dispersion of the lyophilizate in a non-aqueous organic solvent in the presence o f a substrate for the enzyme.
Li Yuh~eh; Li Su-Chen UNITED STATES
Metairie, LA,
A sialidase capable of cleaving a glycoconjugate to yield 3-deoxy-D-glycero-D-galacto2-nonulosonic acid (KDN) is isolated from hepatopancreas of mollusks. Preferably, the sialidase is isolated by processing crude oyster hepatopancreas to form a crude extract of the sialidase enzyme. The crude enzyme is further concentrated and refined utilizing sequential column chromatography fractogel EMD DEAE-650 (M), sephacryl S-200, and fractogel EMD SP 650 (M) chromatography, respectively. Using this procedure, the sialidase is purified over 155 fold with a 17% recovery. Ferric ion exerts a three fold stimulation in the activity of the sialidase, at a concentration of 3 mM. The sialidase cleaves 4-methylumbelliferyl-KDN, KDN alpha2 right arrow3Gal betal right arrow4GlcCer, KDN alpha2 right arrow6Gal betal right arrow4GlcCer, or KDN alpha2 right arrow6GalNAc-ol to yield KDN.
5449661 ANGIOTENSIN CONVERTING ENZYME INHIBITOR AND METHOD FOR PREPARING SAME Nakamura Yasunor; Takano Toshiaki Yokohama, JAPAN assigned to The Calpis Food Industry Co Ltd An angiotensin converting enzyme inhibitor contains as an effective constituent VaI-Pro-Pro and contains 3 to 10 amino acid residues. A method for producing the aforementioned angiotensin converting enzyme inhibitor involves fermenting a foodstuff material containing VaI-Pro-Pro as a constituent component with lactic acid bacteria.