Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1975-7-2
pubmed:abstractText
A fragment, A-II, isolated from a component of a tryptic digest of bovine growth hormone has growth-promoting activity in rats and metabolic activity in humans similar to human growth hormone. The amino acid sequence of this peptide has been reinvestigated and revised. The 38-amino acid peptide was cleaved with cyanogen bromide, chymotrypsin, and trypsin. The amino acid sequences were then established by Edman degradation as well as with overlapping peptides; Homology in the sequence was good between this bovine growth hormone fragment and peptides occurring in ovine growth hormone, human growth hormone, and human chorionic somatomammotropin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2510-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Studies on the common active site of growth hormone. Revision of the amino acid sequence of an active fragment of bovine growth hormone.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.