Enzymic Degradation of Pectic Acid Part XIII

Enzymic degradation of heparin.

A sulphamidase and a sulphoesterase were isolated from adapted cells of Flavobacterium heparinum. These enzymes were partially purified from the 'heparinases' present in the bacterial extracts and characterized. The sulphamidase has a high specificity for glucosamine N-sulphate and glucosamine 2,6-disulphate. The activity decreases sharply with increasing molecular weight ofthe substrates teste...

The Enzymic Degradation of Adenosinetriphosphate

Hume, E. M. & Krebs, H. A. (1949). Spec. Rep. Ser. med. Res. Coun., Lond., No. 264. Husain, M. A. & Mathur, C. B. (1936). Indian J. Agric. Sci. VI, 591. Karrer, P. & Wiirgler, E. (1943). Hdv. chim. Acta. 26, 118. Kuhn, R. & Lederer, E. (1933). Ber. dtech. chm. Gee.66,488. Lederer, E. (1935). Les Carotenoide de Animaux. Paris: Hermann. McCay, C. M. (1938). Phy8iol. Zool. 11, 89. Mann, T. B. (194...

Hæmatological Technique. Part XIII

Pectic Acid Lyases of Bacillus polymyxa 1

Four enzymes were separated from an extracellular preparation of Bacillus polymyxa by carboxymethylcellulose column chromatography. The pH optima were 8.3 to 8.5, 8.7 to 8.9, 9.2 to 9.4, and 9.5 to 9.6. All of the enzymes required calcium ion for maximum activity, whereas strontium ion was only partially effective in stimulating activity. Cobalt was the only other cation tested which was effect...

Enzymic oxidation of formic acid.

Interest in the metabolic fate of formic acid has been renewed as the result of recent experiments showing active incorporation of carbon-labeled formate into normal body constituents of the pigeon (l-3) and the rat (4, 5). Prior to these findings, enzymes capable of catalyzing the oxidation of formic acid had been reported, widely distributed in plant and animal tissues (6). Only in the case o...