Linked Life Data

9308889

Source:http://linkedlifedata.com/resource/pubmed/id/9308889

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-10-20
pubmed:abstractText
The C-terminal alpha-amidation of peptides is one of the most important events in prohormone and neuropeptide processing. Peptide amidation is a two-step process catalyzed by peptidylglycine (hydroxylating) monooxygenase (B. A. Eipper et al., 1983, Proc. Natl. Acad. Sci. USA 80, 5144-5148) followed by dismutation of the resultant hydroxylated peptide to peptide amide and glyoxylate, stimulated by alpha-hydroxyglycine amidating dealkylase (K. Takahashi et al., 1990, Arch. Biochem. Biophys. 169, 524-530). Previous reports on peptidylglycine monooxygenase from bovine pituitary have generated substantial disagreement as to its molecular size. We have reinvestigated the purification of this enzyme and we find that peptidylglycine monooxygenase activity from fresh bovine pituitary is entirely due to a previously unrecognized catalytic function of growth hormone (somatotropin).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
345
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Identity of bovine growth hormone and peptidylglycine monooxygenase.
pubmed:affiliation
Department of Biochemistry, University College Galway, Ireland.
pubmed:publicationType
Journal Article