FRACTIONATION AND PURIFICATION OF THE THIOL PROTEINASES FROM PAPAYA LATEX

被引:10
作者
DEKEYSER, PM
DESMEDT, S
DEMEESTER, J
LAUWERS, A
机构
[1] Laboratories for General Biochemistry and Physical Pharmacy, Department of Pharmaceutics, University of Ghent, 9000 Ghent
来源
JOURNAL OF CHROMATOGRAPHY B-BIOMEDICAL APPLICATIONS | 1994年 / 656卷 / 01期
关键词
D O I
10.1016/0378-4347(94)00083-2
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Three cysteine proteinases, i.e. chymopapain, papaya proteinase IV and proteinase III, were purified to homogeneity from papaya latex using a combination of ion-exchange chromatography and hydrophobic interaction chromatography. During the purification procedure, the thiol-groups of the active center were reversibly blocked as mixed disulfides with 2-thiopyridone. Homogeneity was proved electrophoretically by native polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate (SDS)-PAGE and rechromatography on a Mono S 5/5 column at pH 5.0.
引用
收藏
页码:203 / 208
页数:6
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