Linked Life Data

7044004

Source:http://linkedlifedata.com/resource/pubmed/id/7044004

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10-11
pubmed:dateCreated
1982-7-8
pubmed:abstractText
The catalytic properties of depeptidyl aminopeptidase and aminopeptidase isolated from human erythrocytes, and the distribution of their activities in different blood cells were determined. Dipeptidyl aminopeptidase was shown to be of the dipeptidyl aminopeptidase III type, activated by Co2+ and inhibited by EDTA, pCMB and partially by DFP and leupeptin. Aminopeptidase preferred Lys-, Phe-, ARg-, and Met-2-naphthylamides as substrates. It was activated by Co2+ and inhibited by EDTA amastatin, bestatin and leupeptin. Dipeptidyl aminopeptidase III activity and aminopeptidase activity on arginine-2-naphthylamide was higher in the population of younger red blood cells. The same activities were also found in thrombocytes, mononuclear and polymorphonuclear leukocytes in concentrations higher than those in erythrocytes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1489-95
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't