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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1975-7-23
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0008-4018
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
242-7
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1125811-Animals,
pubmed-meshheading:1125811-Biological Assay,
pubmed-meshheading:1125811-Chromatography, Gel,
pubmed-meshheading:1125811-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1125811-Fishes,
pubmed-meshheading:1125811-Hormones,
pubmed-meshheading:1125811-Molecular Weight,
pubmed-meshheading:1125811-Muscles,
pubmed-meshheading:1125811-Neurosecretory Systems,
pubmed-meshheading:1125811-Peptides,
pubmed-meshheading:1125811-Rats
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pubmed:year |
1975
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pubmed:articleTitle |
Studies on molecular weights of two peptide hormones from the urophysis of white sucker (Catostomus commersoni).
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pubmed:publicationType |
Journal Article
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