Nature of the Conversion of Ficus carica Variety Kadota Ficin Component D to Component C. Some Physicochemical Properties of Components C and D

Abstract

Component C can be formed from component D under the experimental conditions used during purification of Ficus carica variety Kadota latex. By use of the inhibitor, sodium p-chloromercuribenzoate, the 2 components have been purified to chromatographic homogeneity. The 2 components have identical molecular weights and amino acid composition. The only difference found between the 2 components is the presence of 3 to 6 more amide groups in component D than in component C. There also appears to be a conformational difference between the 2 since component C is not as acidic, with respect to component D, as would be expected from the comparative amide contents. Conformational differences between the 2 are also indicated by the chromatographic behavior of the 2 in the presence and absence of sodium-p-chloromercuribenzoate.

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

“…As was concluded previously (17) it appears that sodium p-chloromercuribenzoate has additional effects on the chromatographic properties of the enzyme components.…”

“…The explanation for the peculiar behavior of the ficin components on gel filtration is unknown. It does not appear that all ficins show this peculiar behavior since the molecular weights of Ficus carica variety Kadota ficin components C and D determined by gel filtration were similar to those determined by other methods (17).…”

“…However, conditions should exist which would permit the ready interconversion of conformers. We have not seen this with the ficin components with one possible ex-ception (16,17).…”

“…The comparative specificity of proteolytic enzymes can be determined conveniently uninhibited components (24). This is somewhat surprising in view of the marked effect sodium p-chloromercuribenzoate has on the chromatographic pattern of Ficius carica variety Kadota ficin (17).…”

Partial Purification and Characterization of a Phytochrome-degrading Neutral Protease from Etiolated Oat Shoots

“…Such an origin has by no means been demonstrated here. There are many possible sources of heterogeneity (28,29), e.g., autolytic reactions (these could be any of those catalyzed by a "protease").…”