By V. Bennett, P. Cuatrecasas (auth.), P. Cuatrecasas (eds.)
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Extra info for The Specificity and Action of Animal, Bacterial and Plant Toxins
The same amount of protein material was applied to each gradient. Arrow indicates the interphase of linear gradient and isotonic sucrose-Tris buffer. From Chang, Bennett and Cuatrecasas (1975). approach of this procedure is to labei cells with low concentrations of radiolabeled protein (10-50 ng ml- 1 , 10 000 to 20 000 cpm ng- 1 ) prior to homogenization by a five to ten min incubation with intact cells at 4°C, or by in situ perfusion of an organ such as liver. These conditions allow nearly complete binding of choleragen, but are not sufficient for activation of adenylate cyclase.
Thus, the initial toxin-membrane complex in incapable of activation adenylate cyclase, as had been proposed previously (Cuatrecasas, 1973d). It is of interest that such different cells as rat adipocytes and toad erythrocytes exhibit nearly identica! delays of about 30 min (Fig. 19). , 1976). , 1976). 44 The Specificity and Action of Toxins 200 500 ~ 160 400 .!. c: -~ ea. c: ·;;; e ' a. 'E O' ' c: E 'E c: o"'"' E a. o> 300 E 120
D indicated in the table. 1% ( w/v) albumin and 40 pg/ml of liver membrane protein. Specific toxin binding was determined by filtration procedures as described in the text. a 125 bGal, galactose; GlyNAc, N-acetyl-glucosamine. containing sialic acid (gangliosides) (see Fig. 6). 4). 5). 6). 6). Further addition of N-acetylneuraminic acid to GM 1 reduces the inhibitory ability by 40-to 100-fold. 8 pg ml- 1 ) and GM 3 (50 pg ml- 1 ) (Cuatrecasas, 1973b ). -o NANA Fig. 6 Structures of some commonly occurring gangliosides.