Papain, the cysteine proteinase, from dried papaya latex was purified by ammonium sulphate fractionation followed by agarose mercurial chromatography. The enzyme was further purified by covalent chromatography on thiol-Sepharose column in order to obtain 95-100% pure form. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis with or without sodium dodecyl sulphate. The enzyme had a molecular weight of 23, 400 as determined by SDS-polyacrylamide gel electrophoresis. He reactions with 2,2'-dipyridyl disulphide and dithiobisnitrobenzoic acid showed that highly active papain contains one-SH group per enzyme molecule.
ZULFAQAR ALAM KHAN ,AHMAD SAEED ,IKRAM ULLAH KHAN ,
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