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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1989-4-17
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pubmed:abstractText |
Proteolytic enzymes and their protein inhibitors have been studied by chemical modification for over four decades. Modifications have helped to identify the active (and reactive) sites and to understand their mechanisms of interaction. Inactive derivatives of the enzymes form stable complexes with some inhibitors. These inactive enzymes have also been used for affinity chromatographic adsorptions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0300-9084
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1171-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3147709-Animals,
pubmed-meshheading:3147709-Chickens,
pubmed-meshheading:3147709-Chymotrypsin,
pubmed-meshheading:3147709-Ducks,
pubmed-meshheading:3147709-Hydrolysis,
pubmed-meshheading:3147709-Kinetics,
pubmed-meshheading:3147709-Ovomucin,
pubmed-meshheading:3147709-Peptide Hydrolases,
pubmed-meshheading:3147709-Protease Inhibitors,
pubmed-meshheading:3147709-Trypsin,
pubmed-meshheading:3147709-Turkeys
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pubmed:year |
1988
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pubmed:articleTitle |
Reflections on chemical modification of proteinases and their protein inhibitors.
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pubmed:affiliation |
Department of Food Science and Technology, University of California, Davis 95616.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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