Fractionation of toxins from Hydrophis cyanocinctus venom and determination of amino acid composition and end groups of Hydrophitoxin a

Fractionation of toxins from Hydrophis cyanocinctus venom and determination of amino acid composition and end groups of Hydrophitoxin a

Abstracts for Card Indexes 125 Purification of Aphanizomenon Jios-aguae toxin and its chemical and physiological properties : MAKTOOB ALAM, MIYOSIiI...

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Abstracts for Card Indexes

125

Purification of Aphanizomenon Jios-aguae toxin and its chemical and physiological properties : MAKTOOB ALAM, MIYOSIiI IKAWA, J. J. SASNER, JR . and P. J. SAWYER, Toxicon, 1973, 11, 65 . (Departments of Biochemistry and Zoology, University of New Hampshire, Durham, New Hampshire 03824, U .S .A .) . Abstract-A toxin in chromatographically pure form has been isolated from natural blooms of the blue-green alga Aphanizomenon flos-aquae . The toxin is a strongly basic substance, which gives a positive ninhydrin reaction and appears to be a guanidine derivative. A dose of 2~7 Wg injected intraperitoneally into 20 g mice caused death in 4~9 min. The purified toxin reversibly blocks action potentials and tension development in amphibian nerve-muscle preparations withoutalteration of the restingpotential. The toxin differs from saxitoxin in some of itschemical and physical properties, and some of its effects on neuromuscular systems.

Fractionation of toxins from Hydrophis cyanocinctus venom and determination of amino acid composition and end groups of Hydrophitoxin a: C.-S. LIU, G. S. HUBER, C.-S. LIN and R. Q. BLACKWELL, Toxicon, 1973, 11, 73 . (Department of Biochemistry and Toxicology Section, Department of Clinical Investigation, U.S . Naval Medical Research Unit No . 2, Taipei, Taiwan, Republic of China and Publications Office, U.S . Naval Medical Research Unit No . 2, Box 14, APO San Francisco 96263, U.S .A . Abstract-Three toxic fractions were separated from crude venom of the sea snake Hydrophis cyanocinctus by column chromatography. The most abundant fraction, called Hydrophitoxin a, has been studied foraminoacid composition and found to contain 19 of thecommon amino acids (including asparagine and glutamine) ; phenylalanine is absent. The total number of amino acid residues per molecule is estimated to be 59 . Methionine occupies the N-terminal position and asparagine is at the C-terminal end. From these preliminary results Hydrophitoxin a appearsto be similar in molecular siuand structure to several otherseasnake venoms previously reported .

Mechanism of action of purified scorpion toxin on the isolated rat intestine : J. R . CUNHA MELD, L. FREIRE-MAIA, W. L. TAFURI and T. A . MARIA, Toxicon, 1973,11, 81 . (Department of Physiology, Institute of Biological Sciences, UFMG, CP . 2486, and Department of Pathology, Faculty of Medicine, UFMG, Belo Horizonte, MG. Brazil). Abstract-Purified scorpion toxin (Tityus serrulatus) produced wntraction of the isolated rat ileum, followed by an increase in the amplitude of pendular movement and rhythmic variation of toms . These effects may be due to the release of acetylcholine and substance P. Toxin produced relaxation in the atropinized rat duodenum, which was abolished by alpha and beta sympatholytic drugs. The contraction produced by 5-HT in the rat ileum was either decreased or abolished by toxin. In the toxin-treated ileum, nicotine produced only relaxation . The mechanisms of the inhibitory effects of toxin on the contractions produced by S-HT and nicotine are discussed . The relaxation produced by nicotine was abolished by alpha and beta sympatholytic drugs and by ganglionic blocking agents . TOXICON 1973 Vd. 11.