STRUCTURE-FUNCTION RELATIONSHIPS IN CEREBRATULUS TOXIN B-IV
作者： K.M. Blumenthal , W.R. Kem
DOI: 10.1016/B978-0-08-024952-0.50062-4
关键词: Membrane 、 Clostridium difficile toxin B 、 Tyrosine 、 Toxin 、 Neurotoxin 、 Axon 、 Chemistry 、 Biochemistry 、 Residue (chemistry) 、 Tryptophan
摘要: ABSTRACT A series of experiments are described which probe structure-function relationships in Cerebratulus toxin B-IV, a small, crustacean-selective, polypeptide neurotoxin whose primary effect is to greatly prolong the repolarization phase action potential. Nitration specific tyrosine residue, or alkylation tryptophan, shown abolish toxicity without causing gross conformational changes protein. highly radioactive, pharmacologically active derivative B-IV has been prepared, and preliminary studies binding this molecule crustacean axon membranes described.
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