rdf:type |
|
lifeskim:mentions |
umls-concept:C0009208,
umls-concept:C0018670,
umls-concept:C0030956,
umls-concept:C0204727,
umls-concept:C0205409,
umls-concept:C0322514,
umls-concept:C0728938,
umls-concept:C1555707,
umls-concept:C1705851,
umls-concept:C1880022,
umls-concept:C2752151,
umls-concept:C2828366
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pubmed:issue |
1
|
pubmed:dateCreated |
1984-3-29
|
pubmed:abstractText |
Five peptides were isolated by reverse-phase HPLC from head extracts of the cockroach Leucophaea maderae. Four of the peptides were inactivated by aminopeptidase M (APM). The inability of APM to digest the fifth peptide suggests a blocked NH2-terminus. Four of the peptides were inactivated by carboxypeptidase Y (CPY). The activity of the fraction which would have contained proctolin was decreased by about 20%. The complete deactivation of proctolin by CPY indicated that a second peptide, co-eluting with proctolin but refractory to CPY digestion, was responsible for 80% of the biological activity in that fraction. Concentrations of the peptides necessary to produce a threshold response from the isolated cockroach hindgut ranged from 0.009 to 0.083 head equivalents/ml.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD13,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, Immobilized,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/proctolin,
http://linkedlifedata.com/resource/pubmed/chemical/serine carboxypeptidase
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pubmed:status |
MEDLINE
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pubmed:issn |
0742-8413
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
77
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6141862-Aminopeptidases,
pubmed-meshheading:6141862-Animals,
pubmed-meshheading:6141862-Antigens, CD13,
pubmed-meshheading:6141862-Carboxypeptidases,
pubmed-meshheading:6141862-Chromatography, High Pressure Liquid,
pubmed-meshheading:6141862-Cockroaches,
pubmed-meshheading:6141862-Enzymes, Immobilized,
pubmed-meshheading:6141862-Female,
pubmed-meshheading:6141862-Head,
pubmed-meshheading:6141862-Hot Temperature,
pubmed-meshheading:6141862-Intestines,
pubmed-meshheading:6141862-Male,
pubmed-meshheading:6141862-Neuropeptides,
pubmed-meshheading:6141862-Oligopeptides,
pubmed-meshheading:6141862-Peptides,
pubmed-meshheading:6141862-Protein Denaturation,
pubmed-meshheading:6141862-Stimulation, Chemical
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pubmed:year |
1984
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pubmed:articleTitle |
Isolation and partial characterization of five myotropic peptides present in head extracts of the cockroach Leucophaea maderae.
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pubmed:publicationType |
Journal Article
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