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Composition and Properties of a Highly Purified Toxohormone Preparation^*

Kazuo Yunoki and A. Clark Griffin

( Department of Biochemistry, University of Texas M. D. Anderson Hospital and Tumor Institute, Houston, Texas)

The amino acid and lipide composition of a highly active toxohormone preparation (TH₂) from human malignant tissues was investigated. Approximately 80 per cent of the TH₂ could be accounted for as polypeptide, with leucine, alanine, glutamic, and aspartic acid being present in the highest concentrations. The remaining 20 per cent consisted largely of phospholipides.

The TH₂ fraction was divided into various subfractions both by paper chromatographic procedure as well as careful fractionation by use of Amberlite XE-64 columns. Most of the subfractions had approximately the same liver catalase-depressing potency as the TH₂. The N-terminal amino acid of the various subfractions of TH₂ was shown to be arginine. The minimum molecular weights calculated from the N-terminal arginine ranged from 4200 to 6400. It would thus appear that there are several closely related proteolipides of relatively low molecular weight, all possessing toxohormone activity.

From this study we believe that toxohormone activity requires the presence of both a polypeptide and a lipide (probably a phospholipide) component. Acid or enzymatic hydrolysis almost completely destroyed the toxohormone activity, indicating that the peptide is essential. Conclusive evidence as to the absolute necessity of a lipide component for toxohormone activity has not been obtained.

^* Supported by research grants from the Robert A. Welch Foundation and the American Cancer Society, P-26A and 209-A. We are indebted to Dr. B. G. Creech, Methodist Hospital, for carrying out the lipide analysis, and to Dr. J. M. Prescott and Mr. W. T. Williams, Department of Biochemistry, Agricultural and Mechanical College of Texas, for the amino acid analysis on the TH₂ preparation.

On leave from Department of Internal Medicine, Kagoshima University School of Medicine, Kagoshima, Japan.

Received 10/20/60.

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