Linked Life Data

3983902

Source:http://linkedlifedata.com/resource/pubmed/id/3983902

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-5-16
pubmed:abstractText
The relative ability of bovine alpha- and beta-thrombin to hydrolyze selected anilide and ester substrates in presence and absence of monovalent cations has been evaluated. The hydrolysis of both TosGlyProArgpNA and H-D-PhePipArgpNA by either alpha-thrombin or beta-thrombin is more effective in the presence of 0.1 M NaCl than in the presence of 0.1 M KC1. The hydrolysis of BzArgpNA by alpha-thrombin was less effective in the presence of sodium ions than in the presence of potassium ions. The hydrolysis of this latter substrate by beta-thrombin was similar in the presence of either sodium ions or potassium ions. These results suggest that the ionic composition of the solvent affects that catalytic efficiency of alpha-thrombin and beta-thrombin in different ways dependent on the nature of the substrate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Effect of monovalent cations on bovine alpha- and beta-thrombin: importance of substrate structure.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.