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Multiple Molecular Forms of Ficus glabrata Ficin. Their Separation and Relative Physical, Chemical, and Enzymatic Properties ^1,2

^a Department of Food Science and Technology, University of California, Davis, California 95616

Six of the proteolytic enzyme components of Ficus glabrata ficin have been isolated and shown to be chromatographically homogeneous. The molecular weights, the amino acid compositions, the electrophoretic and chromatographic behavior of the tryptic peptides, and the relative specificities of these 6 components have been determined. Within the experimental precision of the methods all 6 components are identical. They also have identical solubilities in sodium chloride and ammonium sulfate solutions. However, they are markedly different in their chromatographic properties. These multiple molecular forms of Ficus glabrata ficin may differ only in their conformational forms (conformers) or they may have minor differences in amino acid sequences which are sufficient to give different conformations and yet not be detected by the usual peptide mapping techniques. At the moment, we favor the latter possibility.

¹ This investigation was supported in part by the National Institutes of Health (GM-05216).

² Taken in part from the dissertation submitted by Don C. Williams to the Graduate Division, University of California, Davis, in partial satisfaction of the requirements for the Ph.D. degree.