Blomhotin: a novel peptide with smooth muscle contractile activity identified in the venom of Agkistrodon halys blomhoffii
A novel peptide has been isolated from the venom of Agkistrodon halys blomhoffii using a bioassay that monitors the stimulant effect on rat stomach fundus. The 11-amino acid peptide, named blomhotin, was purified to homogeneity by gel-filtration column chromatography and reverse-phase HPLC. The amin...
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Published in | Toxicon (Oxford) Vol. 37; no. 12; pp. 1761 - 1770 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
01.12.1999
Elsevier Science |
Subjects | |
Online Access | Get full text |
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Summary: | A novel peptide has been isolated from the venom of
Agkistrodon halys blomhoffii using a bioassay that monitors the stimulant effect on rat stomach fundus. The 11-amino acid peptide, named blomhotin, was purified to homogeneity by gel-filtration column chromatography and reverse-phase HPLC. The amino acid sequence of blomhotin was determined to be pGlu-Gly-Arg-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Arg, which is similar to that of bradykinin-potentiating peptides which themselves cause no contraction of smooth muscle. The contraction induced by blomhotin showed homologous desensitization, implicating the involvement of a blomhotin-specific site in the response. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0041-0101 1879-3150 |
DOI: | 10.1016/S0041-0101(99)00117-8 |