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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1975-11-7
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pubmed:abstractText |
1. The influence of serum on the elastolytic and esterolytic activity of elastase has been studied. With both substrates the inhibition curves are linear. 1 ml of normal human serum inhibits the activity of 0.77 mg of pure porcine elastase. 2. Elastase binds faster with alpha2-macroglobulin (k = 3.4-10(6) M-1 S-1) than it does with alpha1-antitrypsin (k = 5-10(5) M-1 S-1). 3. The dissociation constant of the alpha-antitrypsin -elastase complex is much lower than that of the alpha2-macroglobulin-elastase complex but both complexes are very stable (Ki less than 10(-10) M). 4. Protein pi (inter-alpha-inhibitor) does not inhibit elastase.
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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 |
Jul
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pubmed:issn |
0009-8981
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43-53
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:1080087-Animals,
pubmed-meshheading:1080087-Binding Sites,
pubmed-meshheading:1080087-Blood Proteins,
pubmed-meshheading:1080087-Chromatography, Gel,
pubmed-meshheading:1080087-Humans,
pubmed-meshheading:1080087-Kinetics,
pubmed-meshheading:1080087-Macroglobulins,
pubmed-meshheading:1080087-Mathematics,
pubmed-meshheading:1080087-Pancreas,
pubmed-meshheading:1080087-Pancreatic Elastase,
pubmed-meshheading:1080087-Protein Binding,
pubmed-meshheading:1080087-Swine,
pubmed-meshheading:1080087-alpha 1-Antitrypsin
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pubmed:year |
1975
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pubmed:articleTitle |
On the inhibition of elastase by serum. Some distinguishing properties of alpha1-antitrypsin and alpha2-macroglobulin.
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pubmed:publicationType |
Journal Article
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