Linked Life Data

1216761

Source:http://linkedlifedata.com/resource/pubmed/id/1216761

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1976-4-19
pubmed:abstractText
Partially purified low molecular component, which inhibited the carboxypeptidase N activity in samples with hippuryl-L-lysine and bradikinine as substrates, was isolated from human blood serum by means of chromatography on DEAE-Sephadex, ultrafiltration of the fractions obtained through Amicon membranes UM-10 or UM-2 and subsequent gel filtration through Sephadex G-10. The probable molecular weight of the inhibitor was 2000. The inhibitor was thermolabile; its inhibitory activity was decreased by 50% after 30 min boiling in 0.01 M phosphate buffer, pH 7.8. Trypsin and chymotrypsin did not influence the inhibitory properties of the factor. Hydrolysis of the low molecular component in 6 N HCl at 110 degrees C within 18 hrs and subsequent studies of the amino acid composition showed a number of amino acids in the hydrolysate; the hydrolysate exhibited the inhibitor activity of the initial substance.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0042-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-22
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
[Isolation, purification and properties of a carboxypeptidase inhibitor from human blood serum].
pubmed:publicationType
Journal Article, English Abstract