Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1975-7-23
pubmed:abstractText
The molecular weights of two active principles extracted from the urophysis of the teleost fish Catostomus commersoni in 0.1 N HC1 or in 0.25% acetic acid have been investigated by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis. Two peptides with urotensin I Tlong-acting rat hypotensive) activity and two peptides with urotensin II (fish smooth muscle stimulating) activity were found by these procedures. The smaller of the two urotensin I peptides (molecular weight 1200-1700), designated urotensin Is, was shown to be a fragment of the larger peptide (molecular weight 2300-3000) which is produced by acid hydrolysis withour loss of rat hypotensive activity. The two urotensin II peptides are suggested to represent either a monomer and a dimer or open and closed forms of a peptide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0008-4018
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
242-7
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Studies on molecular weights of two peptide hormones from the urophysis of white sucker (Catostomus commersoni).
pubmed:publicationType
Journal Article