Linked Life Data

6771256

Source:http://linkedlifedata.com/resource/pubmed/id/6771256

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1980-9-28
pubmed:abstractText
Aminotripeptidase [EC 3.4.11.4] was purified from monkey brain by a five-step procedure comprising extraction from brain homogenate, ammonium sulfate fractionation, DEAE-cellulose chromatography, hydroxylapatide chromatography, and Sephadex G-200 gel filtration. A purification of 1,100-fold over the homogenate was achieved and the yield was 12%. The purified enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis at pH 8.9. The amino acid composition of the enzyme resembled that of the pig kidney enzyme. The molecular weight of the enzyme was estimated to be about 65,000 by gel filtration on Sephadex G-200 and 70,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The pH optimum for L-leucyl-glycyl-glycine was about pH 7.5. The enzyme hydrolyzed only tripeptides to yield the NH2-terminal residues as free amino acids and the residual dipeptides. The enzyme did not show activities of arylamidase or carboxypeptidases A and B. The enzyme was inhibited by PCMB, o-phenanthroline, and bestatin. The inhibition by bestatin was competitive and the K1 value was calculated to be 5 X 10(-7) M.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1403-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Isolation and characterization of aminotripeptidase from monkey brain.
pubmed:publicationType
Journal Article