Tosicon, 1973, Vol. 11, pp . 513-5]5 . Petgamon Prcss. Printed in Great Britain

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FRO60LONO, M. F., Pewt.owstia, R., Ctunnts, B. L., Cottsus>Ex, C., ABwuss, M. and JOxFS,J., III. (Mt. Sinai Hospital Cleveland, Pulmonary Research Laboratory, Cleveland, Ohio44106, U.S.A .). Lung surface-active fraction as a model system for macromolecular

ultrastructural studies with Crotales atrox venom. J. LipidRes. 14, 110, 1973 .

Tt~ noo lung surfaco-active fntction and phosphatidylcholine constituents were subjected to hydrolysisby Crotales atrox phospholipase A,. Relative rates of hydrolysis were : dipahnitoyl glyoerophosphoryl-choline > phasphatidylcholine isolated from the surface-active fraction > phosphatidylcholine as anintegral component of the intact sudaoe-active macromokcular structuro. Cholesterol markedly inhibited,whereas tripalrnitin increased, the rate of hydrolysis with both puns phosphatidylcholine substrates. Theeffect of temperature on the velocity indicated the enzyme was most active when the substrates were in thegel state. These kinetic results, in conjunction with audace chemistry studies, can be interpreted to indicatethat the phosphatidylcholine in the intact surface-active macromolecular particle is liquid crystalline dueto molecular interactions with other constituents . Gas-liquid chromatographic analysis of the 2-lysophos-phatidylcholines and fatty acids produced from the enzymatic hydrolysis of the intact surface-active fractionindicated that palmitoyl residues wens more accessible to the enzyme, perhaps because they occupiedpositions near the surface of the particle.

W.F.K.

FkYtct trrm, L. and Fy+tctat, D. (University of Uppsala, Institute of Biochemistry, Uppsale75121, Sweden). Complete amino acid sequence of a nonneurotoxic hemolytic protein fromthe venom ofHaemachattah~»mchates (African Ringhals Cobra) . BlocJtemistry 12, 661,1973 .

TttE ool~i>rze amino acid sequence of the non-neurotoxic, hemolytic, basic protein 12B from the venomof Hamrachatus haemachates is described. The protein consists of 61 amino acids, cross-linked by fourdisulfide bridge, molecular weight 6841 from amino acid composition. Tlr~ cyanogen bromide fragmentsand chymotryptic and tryptic peptides wens separated by gel filtration on Sephadex G-SO or G-25 and zoneelectrophoresis on a cellulose column . The sequence was determined by Edman degradation using the directphenylthiohydantoin method, and carboxypeptidase A. The basic protein 12B is shown to be homologousto other types of proteins, cardiotoxins, and rteurotoxins, and is in the same size range from Elapid venom.

W.F.K .

OMORI-SATOH, T., Swnwtmto, S., OHSnrcA, A. and Mutuze, R. (2nd Department of Bacterio-logy, National Institute of Health, Shinagawa-ku, Tokyo 141, Japan) . Purification andcharacterization of an antihemorrhagic factor in the serum of 7lrimereserus Jiavovlrldis, a

taotalid . Blochlm. biop/rys. Acta 286, 414, 1972.Alv Atvzgt>~oaxxnotc factor in the serum of Trfmereseres jlavovlridis, a crotalid, was purified 21-fold witha yield of 15 per cent . The preparation was homogeneous as judged by ultracentrifugation, gel filtration onSephadex G-200, disc electrophoresis, immunoelectrophoreia and isoelectric focusing. The purified serumfactor inhibited the two immunologically different hemorrhagic principles, HRl and Hlt2, in the venomof this snake, and also the lethal toxicity of the venom. The molecular weight of the purified factor wasabout 70,000, and the isoelectric point around 4.

The crude serum from T.Jlavovlridis inhibited hemorrhagic activities ofvarious snake vraoms, includingCrotalidae, Vlperidae and Elapldae venom. The presence of a common antihemorrhagic substanoe(s) inthe serum ofdifferent species of snakes is suggested.

P.RS.

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