Studies on proteinases from Calotropis gigantea latex. I. Purification and some properties of two proteinases containing carbohydrate.
Two proteinase containing carbohydrate, called calotropain-FI and calotropain-FII, were purified from Calotropis gigantea latex by CM-Sephadex C-50 chromatography. Both calotropain-FI and FII were found to be homogeneous by rechromatography on CM-Sephadex C-50, gel filtration on Sephadex G-100, electrophoresis on polyacrylamide gel and by N-terminal amino acid analysis. Some properties of these enzymes are reported.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D010944:Plants / Q000201:enzymology*; D012408:Rubber
D000596:Amino Acids; D002241:Carbohydrates; D007527:Isoenzymes; D012408:Rubber; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C019809:calotropain-FI; C019810:calotropain-FII