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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1984-9-7
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pubmed:abstractText |
The effects of pH on salt stimulation of the rates of hydrolysis of three substrates by human leukocyte elastase were studied. The enzyme was most active at pH 10.5, 8.0-8.5, and 9.5 for the hydrolyses of fluorescein isothiocyanate-labeled S-carboxymethylated bovine serum albumin (FITC-CM-BSA), succinyl-L-Ala-L-Pro-L-Ala-7-methylcoumaryl-4-amide (Suc-APA-MCA), and succinyl-L-Ala3-p-nitroanilide (Suc-Ala3-pNA), respectively, in the absence of NaCl. The enzyme was activated by 0.5 M NaCl similarly at all pHs tested for the hydrolysis of Suc-Ala3-pNA, but more at neutral and alkaline pH values, respectively, for the hydrolyses of FITC-CM-BSA and Suc-APA-MCA. Thus, in the presence of 0.5 M NaCl, the enzyme was most active at pH 8.0 and 10.0 with FITC-CM-BSA and Suc-APA-MCA, respectively. In contrast, the proteolytic activity of porcine pancreatic elastase was somewhat inhibited by 0.5 M NaCl.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
233
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
212-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6565481-Enzyme Activation,
pubmed-meshheading:6565481-Humans,
pubmed-meshheading:6565481-Hydrogen-Ion Concentration,
pubmed-meshheading:6565481-Kinetics,
pubmed-meshheading:6565481-Leukocytes,
pubmed-meshheading:6565481-Osmolar Concentration,
pubmed-meshheading:6565481-Pancreatic Elastase,
pubmed-meshheading:6565481-Salts,
pubmed-meshheading:6565481-Substrate Specificity
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pubmed:year |
1984
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pubmed:articleTitle |
pH dependence of salt activation of human leukocyte elastase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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