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Titlebook: Animal, Plant, and Microbial Toxins; Volume 2 Chemistry, Akira Ohsaka,Kyozo Hayashi,Nobuo Tamiya Book 1976 Springer Science+Business Media

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發(fā)表于 2025-3-21 18:02:57 | 只看該作者 |倒序瀏覽 |閱讀模式
期刊全稱Animal, Plant, and Microbial Toxins
期刊簡稱Volume 2 Chemistry,
影響因子2023Akira Ohsaka,Kyozo Hayashi,Nobuo Tamiya
視頻videohttp://file.papertrans.cn/158/157694/157694.mp4
圖書封面Titlebook: Animal, Plant, and Microbial Toxins; Volume 2 Chemistry,  Akira Ohsaka,Kyozo Hayashi,Nobuo Tamiya Book 1976 Springer Science+Business Media
影響因子During the past two decades, research on animal, plant, and microbial toxins has expanded rapidly, and new and exciting information has appeared to clarify both the clinical and therapeutic aspects of intoxication and, even more impor- tant, to help us understand more exactly the structure and the mode of action of toxins on a molecular basis. Because of the interdisciplinary nature of toxin research, it is of vital impor- tance that workers specializing in its different aspects should make a particular effort to exchange and keep up with new developments in this rapidly-expanding field. This has been one of the main purposes of the series of international meetings that have been held over the past ten years. The increasing interest in the results of toxin research can be explained partly by the growing general preoccupation with pollution and its toxic effects, which means that more anq more specialists in other fields are finding it necessary to keep in touch with current research into naturally occurring toxins. The papers in these volumes were presented at the Fourth International Symposium on Animal, Plant and Microbial Toxins, organized by the Inter- national Society on Toxic
Pindex Book 1976
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Structural Nature of Presynaptic Neurotoxins from the Venoms of the Australian Tiger Snake, ,, and tnergic neuromuscular junction either by (1) a postsynaptic curarelike action on the nicotinic acetylcholine receptors of the muscle motor endplate, or (2) a presynaptic interference with the release of acetylcholine from the motor nerve terminals.
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Isolation and Amino Acid Sequence of Proteinase Inhibitors from the Venoms of , and ,ypsin (Takahashi . 1972),. Such proteinase, inhibitors are distributed mainly in the venoms of members of . and . (Takahashi .., 1974a). One of the inhibitors, inhibitor II, isolated from . venom is a polypeptidic substance, consisting of 60 amino acid residues. Its established primary strucutre is
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Complete Amino Acid Sequence of Snake Venom Phospholipase A2idely distributed in the venoms of snakes, bees, and scorpions as well as in animal tissues. Recently, a number of forms of phospholipase A. have been highly purified from various species of . (Braganca .., 1969; Salach .., 1971; Shiloah .., 1973a,b; Wahlstr?m, 1971; Sakhibov .., 1970; Lo and Chang,
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Synthetic Studies of α-Bungarotoxinnsmission mechanisms. In view of this, an urgent problem was the relationship among the primary structure, conformational states, and biological properties of the neurotoxins, which together would serve as basis for understanding their mode of action at the molecular level. In our opinion, the progr
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Structure and Function of Ricin Datography at pH 8.5 and crystallized in the presence of 10. M cupric ion (Ishiguro.., 1971a). Terminal analysis of ricin D, giving He and Ala at N-termini and Ser and Phe at C-termini, suggested that ricin D consists of two peptide chains (subunits) (Ishiguro .., 1971b). After performic acid oxidati
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The Amino Acid Sequence of the Staphylococcal Enterotoxinsfood poisoning. The ingestion of these substances by humans produces a variety of symptoms, the most common being vomiting and diarrhea in 2–6 hr. Although this illness is not a reportable disease in the United States, a large percentage of food-borne illnesses that are reported are caused by the in
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