Linked Life Data

547740

Source:http://linkedlifedata.com/resource/pubmed/id/547740

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-8-15
pubmed:abstractText
Lysosomes (granules) of rabbit PMN leukocytes were extracted with either HCl or H2SO4, and the extracts were chromatographed over Sephadex to separate protein constituents. Some of the low molecular weight cationic proteins homogeneous on SDS PAGE (8% and 12.5% gels) were characterized by electrophoretic mobility in acid gels and by amino acid analysis. A 3,700 dalton polypeptide, rich in arginine and cysteine, prolonged the partial thromboplastin time of normal plasma. In low concentration, this protein shortened the clotting time of pure fibrinogen by thrombin. In high concentration this lysosomal cationic protein precipitated fibrinogen from solution; no fibrinopeptides were released to suggest cleavage of fibrinogen. Fibrinolytic protease activity was detected in crude H2SO4 extracts but not in crude HCl extracts. Two separate plasminogen activators, differing from kallikrein or prekallikrein, were isolated from the H2SO4 lysosomal extract and were partially characterized; neither exhibited proteolytic activity on fibrinogen free of plasminogen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0361-8609
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-79
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Isolation and characterization of granulocyte lysosomal proteins and study of their effects on the clotting system.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.