Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-10-12
pubmed:abstractText
A low calcium requiring form of calcium activated neutral protease (mu-CANP) was purified to homogeneous state from a soluble fraction of human platelets. The purified protease was composed of two subunits of 80 K and 25 K proteins, judged by SDS polyacrylamide gel electrophoresis and the approximate molecular weight of 105 K was also confirmed by gel filtration technique. The purified enzyme was activated in the presence of micromolar concentration off Ca2+ and also activated with other divalent cations such as Sr2+, Ba2+, Mn2+, Ni2+. Leupeptin, antipain, an epoxysuccinate derivative (E-64), and alkylating agents were potent inhibitors of the purified enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-80
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification and characterization of a low calcium requiring form of Ca2+-activated neutral protease from human platelets.
pubmed:publicationType
Journal Article