Linked Life Data

2177163

Source:http://linkedlifedata.com/resource/pubmed/id/2177163

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-2-28
pubmed:abstractText
An endopeptidase generating fragment (1-5) from luteinizing hormone-releasing hormone (LHRH) has been solublized with Brij 35 from neuroblastoma cell membrane and purified by a procedure including p-mercuribenzoate-Sepharose chromatography, Mono-Q high-performance liquid chromatography and Superose 6 gel filtration. The molecular weight of the enzyme was estimated to be 100,000 by gel filtration. LHRH fragment (1-5)-generating activity of the enzyme was strongly inhibited by metal-chelating and sulfhydryl-blocking reagents. An enzyme with similar properties to those of the neuroblastoma enzyme was also purified from rat brain synaptic membranes. The properties of the two purified enzymes corresponded to those of a thiol-dependent protease proposed to be the enzyme responsible for the initial cleavage of LHRH by neuroblastoma cell membranes and rat brain synaptic membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0143-4179
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Thiol-dependent membrane-bound metallo-endopeptidase functioning in degradation of luteinizing hormone-releasing hormone in neuroblastoma cells and rat brain synaptic membrane. Isolation and characterization.
pubmed:affiliation
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't