AMINO-ACID-SEQUENCE OF TOXIN-I FROM ANEMONIA-SULCATA

被引：59

作者：

WUNDERER, G ^{[1
]}

EULITZ, M ^{[1
]}

机构：

[1] GESELL STRAHLEN & UMWELTFORSCH MBH,INST HAMATOL,IMMUNOL ABT,LANDWEHRSTR 61,D-8000 MUNCHEN 2,FED REP GER

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1978年 / 89卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1978.tb20890.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Toxin I from Anemonia sulcata, a major component of the sea anemone venom, consists of 46 amino acid residues which are linked by three disulfide bridges. The [14C]carboxymethylated polypeptide was sequenced to position 29 by automated Edman degradation. The remaining sequence was determined from cyanogen bromide peptides and from tryptic peptides of the citraconylated [14C]carboxymethylated toxin. Toxin I is homologous to toxin II from Anemonia sulcata and to anthopleurin A, a toxin from the sea anemone Anthopleura xanthogrammica. These toxins constitute a new class of polypeptide toxins. No significant homologies exist with toxin III from Anemonia sulcata nor with known sequences of neurotoxins or cardiotoxins of various origin. Copyright © 1978, Wiley Blackwell. All rights reserved

引用

页码：11 / 17

页数：7

共 22 条

[1]

ALSEN C, TOXICON

[2]

Atassi M Z, 1972, Methods Enzymol, V25, P546, DOI 10.1016/S0076-6879(72)25053-4

[3] ISOLATION AND CHARACTERIZATION OF 3 POLYPEPTIDES WITH NEUROTOXIC ACTIVITY FROM ANEMONIA-SULCATA [J].