STUDIES ON PROTEINASES FROM CALOTROPIS-GIGANTEA LATEX .2. PHYSICOCHEMICAL PROPERTIES OF CALOTROPAIN-FI AND CALOTROPAIN-FII

The molecular weights of purified calotropain-FI and FII were determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and by gel filtration on Sephadex G-100. Activation of calotropain-FI and FII by different sulfhydryl activators was studied. The results obtained from inhibition studies by various enzyme-modifying reagents suggest the possible role of cysteine and histidine residues in the active site of both the enzymes. The free and total sulfhydryl contents of both the enzymes were determined by the use of 5-5′-dithio-bis-2-nitrobenzoic acid. Total amino acid compositions of both the enzymes were also determined. A comparative study of the esterase, amidase, milk-clotting and caseinolytic activities of calotropain-FI and FII are also presented. © 1979.