COMPLETE AMINO-ACID-SEQUENCE OF TENEBROSIN-C, A CARDIAC STIMULATORY AND HEMOLYTIC PROTEIN FROM THE SEA-ANEMONE ACTINIA-TENEBROSA

被引：62

作者：

SIMPSON, RJ ^{[1
]}

REID, GE ^{[1
]}

MORITZ, RL ^{[1
]}

MORTON, C ^{[1
]}

NORTON, RS ^{[1
]}

机构：

[1] UNIV NEW S WALES,SCH BIOCHEM,KENSINGTON,NSW 2033,AUSTRALIA

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 190卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb15579.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：

The complete amino acid sequence of the cardiac stimulatory and haemolytic protein tenebrosin‐C, from the Australian sea anemone Actinia tenebrosa, has been determined by Edman degradation of the intact molecule and fragments produced by treatment of the polypeptide chain with cyanogen bromide and enzymatic cleavage with endoproteinase Asp‐N, thermolysin and trypsin. The molecule is a single‐chain polypeptide consisting of 179 amino acid residues with a calculated molecular mass of 19 797 Da. Tenebrosin‐C shows a high degree of amino acid sequence similarity (63%) with Stoichactis helianthus cytolysin III [Blumenthal, K. M. and Kem, W. R. (1983) J. Biol. Chem. 258, 5574–5581] and is identical to a partial sequence (90 residues) reported for equinatoxin, a cardiostimulatory and haemolytic protein isolated from the European sea anemone Actinia equina [Ferlan, I. and Jackson, K. (1983) Toxicon Suppl. 3, 141–144]. No amino acid sequence similarity was detected between tenebrosin‐C and other protein sequences stored in available databases. The predicted secondary structure of tenebrosin‐C suggests that it is a compact, highly structured molecule. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：319 / 328

页数：10

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