Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-5-14
pubmed:abstractText
A protein from Drosophila melanogaster which inhibits bovine alpha-chymotrypsin activity was purified using an extensive extraction procedure. SP-Sephadex column chromatography and affinity column chromatography. The inhibitor has an estimated molecular weight of approx. 12 000 and is extremely pH and heat stable. It did not exhibit any inhibitory activity against trypsin from numerous sources nor mosquito larval chymotrypsin but did inhibit adult mosquito chymotrypsin. Chymotrypsin-like activity has not been found in Drosophila and therefore the function of the inhibitor is unknown. Preliminary work indicates that it effectively inhibits cathepsin D activity from a nematode parasite and rabbit liver.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
611
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and partial-characterization of a protease inhibitor from Drosophila melanogaster.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.