Immunology

Animal, Plant, and Microbial Toxins: Volume 2 Chemistry, by Nobuyo Maeda, Nobuo Tamiya, Y. M. Chen, C. Y. Lee (auth.),

By Nobuyo Maeda, Nobuo Tamiya, Y. M. Chen, C. Y. Lee (auth.), Akira Ohsaka, Kyozo Hayashi, Yoshio Sawai, Ryosuke Murata, Masaru Funatsu, Nobuo Tamiya (eds.)

During the earlier 20 years, study on animal, plant, and microbial pollutants has elevated swiftly, and new and intriguing info has seemed to make clear either the scientific and healing features of intoxication and, much more impor­ tant, to aid us comprehend extra precisely the constitution and the mode of motion of poisons on a molecular foundation. end result of the interdisciplinary nature of toxin learn, it's of significant impor­ tance that employees focusing on its varied points may still make a selected attempt to switch and stay alongside of new advancements during this rapidly-expanding box. This has been one of many major reasons of the sequence of overseas conferences which have been held during the last ten years. The expanding curiosity within the result of toxin study could be defined partially through the turning out to be normal preoccupation with toxins and its poisonous results, this means that extra anq extra experts in different fields are discovering it essential to keep up a correspondence with present learn into obviously taking place pollutants. The papers in those volumes have been offered on the Fourth overseas Symposium on Animal, Plant and Microbial pollution, prepared through the Inter­ nationwide Society on Toxicology, held in Tokyo in September, 1974. The editors have determined to incorporate either unique reviews and evaluate articles, prepared in response to disciplines. modifying has been saved to the minimal helpful for sufficient comprehension of the materials.

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Extra info for Animal, Plant, and Microbial Toxins: Volume 2 Chemistry, Pharmacology, and Immunology

Example text

Chromatography on Bio-Rex 70 of fraction 3. 5. 1 M ammonium acetate solution; flowrate, 45 ml/hr. or paper electrophoresis, we could not isolate the 20-membered peptide in amounts sufficient for analysis. However chymotryptic hydrolysis of carboxymethylated neurotoxin I gave us nine peptides which afforded enough information for establishing the amino acid sequence of neurotoxin I (Table 3). Neurotoxin I from N. n. oxiana venom belongs to the group of the so-called long-chain neurotoxins with five intramolecular disulfide bonds.

5-mm pathlength. (c) Gradient chromatography of gel f"lltration fraction Ill. ) Notexin and Taipoxin 33 Table 1. 0 bromide, yielding the fragments 1-8,9-57, and 58-118. Composition data for these and various sub fragments confirm the integral values given in Table 1 for the intact enzyme, which is very similar in amino acid composition to notexin. The basic N. , 1973), but is about 3D-fold less potent. Furthermore, as measured by the titration of fatty acids liberated from egg yolk emulsions, notexin has significant phospholipase activity, about 5% that of the basic N.

1 M NH 4 HC0 3 buffer. In all the other cases, isolation and purification of peptides were done by paper chromatographyand electrophoresis in standard buffer systems. , 1973). N-terminal sequences of the carboxymethylated cytotoxin and its cyanogen bromide fragment were determined on a Beckman model 890 automatic sequencer. , 1971) gave practically homogeneous neurotoxins I and II. Cytotoxin was obtained by chromatography on Bio-Rex 70 of fraction 3 (Fig. 1). Amino acid composition of the neurotoxins and cytotoxin are listed in Table 1.

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