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A simple and rapid purification of kallikrein from rat submandibular gland
T S el-Thaher1, G M Saed, G S Bailey
1Department of Chemistry and Biological Chemistry, University of Essex, U.K.
Biochimica Et Biophysica Acta
|May 16, 1990
Abstract:
Rat submandibular kallikrein was isolated in an 87% yield by a very quick and simple procedure involving hydrophobic interaction chromatography. Furthermore, that purification method was superior to both aprotinin-affinity chromatography and immunoaffinity chromatography for the purification of rat submandibular kallikrein. The kallikrein purified by hydrophobic interaction chromatography consisted of a number of isoenzymes. The major component of Mr 38,000 seen on SDS-gel electrophoresis was found to be the glycosylated kallikrein, whereas the minor component of Mr 26,000 represented the non-glycosylated enzyme.