Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-11-7
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-53
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
On the inhibition of elastase by serum. Some distinguishing properties of alpha1-antitrypsin and alpha2-macroglobulin.
pubmed:publicationType
Journal Article