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Multiple Molecular Forms of Ficus glabrata Ficin. Their Separation and Relative Physical, Chemical, and Enzymatic Properties
Don C. Williams and John R. Whitaker
Vol. 44, No. 11 (Nov., 1969), pp. 1574-1583
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4261877
Page Count: 10
You can always find the topics here!Topics: Enzymes, Amino acids, Latex, Chromatography, Sodium, Molecular weight, pH, Chemical composition, Hydrolysis, Gels
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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.
Plant Physiology © 1969 American Society of Plant Biologists (ASPB)