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Snake venoms. The amino-acid sequence of polypeptide DE-1 from Ophiophagus hannah (King cobra) venom.

Authors :
Joubert FJ
Source :
Hoppe-Seyler's Zeitschrift fur physiologische Chemie [Hoppe Seylers Z Physiol Chem] 1977 May; Vol. 358 (5), pp. 565-74.
Publication Year :
1977

Abstract

A major polypeptide (DE-1) was purified from King cobra venom by ion-exchange chromatography on CM-cellulose and also DEAE-cellulose and by gel filtration on Sephadex G-50. DE-1 comprises 60 amino acid residues and is cross-linked by four intrachain disulphide bridges. The complete primary structure of the polypeptide has been elucidated. The properties of DE-1 were compared with those of the short neurotoxin and the cytotoxin groups and of the angusticeps types. The sequence and some of the invariant residues of DE-1 resemble the short neurotoxin group and to some degree also the cytotoxin group, but it is a nontoxic (LD50 greater than 250 microgram/g of mouse) polypeptide.

Details

Language :
English
ISSN :
0018-4888
Volume :
358
Issue :
5
Database :
MEDLINE
Journal :
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Publication Type :
Academic Journal
Accession number :
881163
Full Text :
https://doi.org/10.1515/bchm2.1977.358.1.565