Linked Life Data

1190618

Source:http://linkedlifedata.com/resource/pubmed/id/1190618

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1976-1-17
pubmed:abstractText
Polymorphonuclear leukocyte lysosomal esterolytic activity on the synthetic substrate, t-butyloxycarbonyl-L-alanine p-nitrophenyl ester was observed to correlate well with polymorphonuclear leukocyte granule elastase activity measured on the natural substrate, elastin, bound to rhodamine. In addition, the effect of highly specific, irreversible chloromethyl ketone elastase inhibitors on leukocyte lysosomal elastase activity was similar, using t-butyloxycarbonyl-L-alanine p-nitrophenyl ester or elastin-rhodamine as substrate. Whether polymorphonuclear leukocyte lysosomal granules contain two different enzymes, a true elastase with esterase activity and a similar esterase without elastase activity, as found in the human pancreas, is, as yet, unknown. Both enzyme activities have been identified in isoenzymes of purified human polymorphonuclear leukocyte lysosomal elastase. The correlations observed between the two enzymes, if present in polymorphonuclear leukocytes, are sufficiently strong to use the esterase assay for clinical purposes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-0805
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
629-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Human granulocyte lysosomal elastase activity using t-butyloxycarbonyl-L-alanine p-nitrophenyl ester and elastin-rhodamine as substrates.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.