HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Blumenthal, K. M. Articles by Kem, W. R. Search for Related Content PubMed PubMed Citation Articles by Blumenthal, K. M. Articles by Kem, W. R. Social Bookmarking                      What's this?

JBC, Vol. 251, Issue 19, 6025-6029, Oct, 1976

Structure and action of heteronemertine polypeptide toxins. Primary structure of Cerebratulus lacteus toxin B-IV

K. M. Blumenthal and W. R. Kem

The amino acid sequence of Cerebratulus toxin B-IV, a crustacean-selective axonal toxin occurring in the marine worm C. lacteus, was determined by Edman degradation of the tryptic and staphylococcal protease peptides obtained from the reduced, carboxymethylated toxin. All four of the anticipated maleylated tryptic peptides, ranging in size from 8 to 23 residues, and three staphylococcal protease peptides, ranging from 9 to 35 residues, were isolated in pure form by gel filtration followed by either ion exchange chromatography or preparative paper electrophoresis. The order of the maleylated tryptic peptides was based upon the sequences of the staphylococcal protease peptides. As might be expected, toxin B-IV displays no homology with the elapid nicotinic receptor toxins. In addition, toxin B-IV is structurally unrelated to a group of scorpion neurotoxins which, like B-IV, affect action potential generating mechanisms.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?