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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1984-3-12
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pubmed:abstractText |
The partitioning of the acylenzyme acetyl-(Gly)n-Phe(NO2)-chymotrypsin (n = 0,1,2) to peptide and peptide acid is observed spectrophotometrically. Values of partitioning ratios for various nucleophiles are calculated from the spectral data. They are a measure for the "true" nucleophile reactivity and are useful in the prediction of the best experimental conditions in enzymic peptide synthesis. A large difference in the nucleophile reactivity is observed which is attributed to the S'2-P'2 interaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
|
pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
118
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
317-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6696760-Animals,
pubmed-meshheading:6696760-Cattle,
pubmed-meshheading:6696760-Chymotrypsin,
pubmed-meshheading:6696760-Indicators and Reagents,
pubmed-meshheading:6696760-Kinetics,
pubmed-meshheading:6696760-Pancreas,
pubmed-meshheading:6696760-Peptides,
pubmed-meshheading:6696760-Substrate Specificity
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pubmed:year |
1984
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pubmed:articleTitle |
Nucleophile specificity in chymotrypsin peptide synthesis.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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