Some problems in cancer research.
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Biomedical subjects
Publications and source records attributed to D C Williams.
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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.
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The latices of only 13 of a total of 46 species of Ficus examined contained appreciable proteolytic activity. Therefore, high proteolytic activity in the latex is not a distinguishing feature of the genus. The latex of F. stenocarpa had the highest specific activity followed closely by the latices of F. carica and F. glabrata. Latices of 6 species of Ficus were examined by chromatography on CM-cellulose and compared with the results obtained for 9 varieties of F. carica. All of the latices were found to contain multiple proteolytic enzymes. Chromatographically, the multiple enzyme components of the several varieties of F. carica were more similar than those of the several species examined. The latices of 16 varieties of F. carica were all different as determined by free boundary electrophoresis although the specific proteolytic activity of the latices was reasonably constant.
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1. Implantation of diethylstilboestrol pellets into adult male rats brings about similar biochemical changes in the nucleic acid and protein metabolism to castration. 2. The avidity of the prostate for labelled diethylstilboestrol was greater than that of the other organs examined. 3. Uptake of labelled diethylstilboestrol and testosterone into the nuclei of the rat prostate is greater in castrated rats than in controls. 4. Diethylstilboestrol appeared to be associated with the protein and not with the DNA fraction of the nucleus.