Linked Life Data

6873305

Source:http://linkedlifedata.com/resource/pubmed/id/6873305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1983-9-20
pubmed:abstractText
This paper presents the results obtained when pig anterior pituitary granule lysates are incubated with rat pro-opiomelanocortin (POMC). The resultant peptides were analyzed by 3 systems of high-performance liquid chromatography. This approach, when coupled with microsequence analysis of the conversion products, allowed the unambiguous identification of a major chymotryptic-like activity (pH optimum around 8) associated with the granule lysates with a specificity directed towards selective Tyr-X and Phe-X bonds within the POMC molecule. Furthermore, these results also demonstrate that although the detected enzyme activity gives rise to products 'resembling' those expected, the characterization of the 'elusive' maturation enzyme responsible for the cleavage at pairs of basic residues remain to be critically evaluated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
68-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Enzymatic cleavage of pro-opiomelanocortin by anterior pituitary granules. Evidence for a chymotryptic-like enzyme.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't