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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-3-28
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pubmed:abstractText |
Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro24 is replaced by Ala24, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.
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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 |
Nov
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pubmed:issn |
0022-0795
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
115
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
R5-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2830360-Adrenal Cortex,
pubmed-meshheading:2830360-Adrenocorticotropic Hormone,
pubmed-meshheading:2830360-Aldosterone,
pubmed-meshheading:2830360-Amino Acid Sequence,
pubmed-meshheading:2830360-Animals,
pubmed-meshheading:2830360-Guinea Pigs,
pubmed-meshheading:2830360-Molecular Sequence Data
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pubmed:year |
1987
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pubmed:articleTitle |
Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells.
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pubmed:affiliation |
Medical Research Centre, Prince Henry's Hospital, Melbourne, Australia.
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pubmed:publicationType |
Journal Article
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