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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1979-11-21
|
| pubmed:abstractText |
The steady-state kinetics of plasmin- (EC 3.4.21.7) and trypsin-catalysed (EC 3.4.21.4) hydrolysis of Bz-L-Phe-Val-Arg-pNA, Bz-D-Phe-Val-Arg-pNA, L-Phe-Val-Arg-pNA, D-Phe-Val-Arg-pNA and D-Val-Leu-Lys-pNA were investigated in the pH range 6-9. The pH dependences of the kinetic parameters correspond with the effects of catalytically essential ionizations in the enzymes, except for reactions with L- and D-Phe-Val-Arg-pNA, in which protonation of the NH2-terminal alpha-amino groups (pK = 7.0) shows some inhibitory effect. The reactions of plasmin and trypsin with p-nitroanilides show kc values similar to those normally found with specific ester substrates, indicating that the deacylation steps of the reactions are rate determining.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
569
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
177-83
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1979
|
| pubmed:articleTitle |
Steady-state kinetics of plasmin- and trypsin-catalysed hydrolysis of a number of tripeptide-p-nitroanilides.
|
| pubmed:publicationType |
Journal Article
|