A simple and rapid purification of kallikrein from rat submandibular gland.
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.
Department of Chemistry and Biological Chemistry, University of Essex, U.K.
T S
TS
el-Thaher
G M
GM
Saed
G S
GS
Bailey
D000818:Animals; D007611:Aprotinin; D002845:Chromatography; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification; D007610:Kallikreins / Q000302:isolation & purification*; D008297:Male; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D013363:Submandibular Gland / Q000032:analysis*
D007527:Isoenzymes; D007611:Aprotinin; D007610:Kallikreins