Affinity chromatographic purification of papain

International Journal of Peptide and Protein Research
M O FunkE T Kaiser

Abstract

The reinvestigation of the affinity chromatographic method of purifying papain has been carried out. It has been reported that papain could be purified by taking advantage of the affinity of the enzyme for the insolubilized peptide inhibitor, agarose-Gly-Gly-Tyr(Bz)-Arg. Using pure tetrapeptide obtained commercially and standard coupling procedures, a significant purification of papain could not be achieved. Both active and nonactivatible enzyme bound to a column prepared in this manner were eluted together by the use of deionized water. An affinity medium with properties similar to those reported by Blumberg et al. was obtained by removal of the benzyl group on tyrosine prior to coupling with agarose. The deprotected tetrapeptide was also synthesized by an independent route and inhibition constants for the binding of the protected and deprotected tetrapeptide to papain were determined in kinetic experiments.

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Citations

Oct 25, 1996·The Journal of Biological Chemistry·V N KalabokisA G Szent-Györgyi
Jun 23, 2011·Organic & Biomolecular Chemistry·Pierre HaquetteMichèle Salmain
Sep 4, 2018·Metallomics : Integrated Biometal Science·Mickaël V CherrierJuan C Fontecilla-Camps
Oct 1, 1994·Journal of Muscle Research and Cell Motility·V N KalabokisA G Szent-Györgyi
Nov 15, 2019·International Journal of Biological Macromolecules·Kahina HafidMohammed Gagaoua
Jan 14, 2020·Bioconjugate Chemistry·Ivan BassaniniSergio Romeo
Jan 1, 1990·Biopolymers·J P Germanas, E T Kaiser
Sep 11, 2018·Inorganic Chemistry·Chandan Kr BarikWeng Kee Leong

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