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Chemical synthesis of a hexadecapeptide segment of ubiquitin that activates adenylate cyclase and induces lymphocytes to differentiate

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Summary

A hexadecapeptide corresponding to positions 59–74 of ubiquitin was synthesized and purified. The peptide was characterized by its mobility in TLC and electrophoresis, amino acid sequence and composition, and molar rotation. The peptide possessed approximately 40% activity compared with native ubiquitin in each of 3 biological assays in vitro: a) thymocyte induction, b) B cell induction and c) elevation of intracellular cyclic AMP levels in sarcoma 180 cells.

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Author information

Authors and Affiliations

  1. Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, 02114, Boston, Massachusetts, USA

    D. H. Schlesinger

  2. Memorial Sloan-Kettering Cancer Center, 10021, New York, New York, USA

    D. H. Schlesinger

  3. Department of Pathology, Yale University School of Medicine, 06510, New Haven, Connecticut, USA

    D. H. Schlesinger

Authors
  1. D. H. Schlesinger
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  2. G. Goldstein
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  3. Margrit P. Scheid
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  4. M. Bitensky
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Additional information

Acknowledgments. We thank Dr Geoffrey Tregear for helpful suggestions for the synthesis strategy, Dr Jim Burton for guidance with the methods for establishing peptide purity, and Ronald King, Miriam Miller, Jeanette Dilley and Linda Townley for excellent technical assistance. This work was supported by U.S. Public Health Service Grants CA-08748, CA-16889, CA-08415, CA-17085 and AI-12487, and by NCI Contract CB-53868.

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Schlesinger, D.H., Goldstein, G., Scheid, M.P. et al. Chemical synthesis of a hexadecapeptide segment of ubiquitin that activates adenylate cyclase and induces lymphocytes to differentiate. Experientia 34, 703–704 (1978). https://doi.org/10.1007/BF01947269

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