Plant Physiol. Drug Metab Dispos
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Plant Physiology 88:770-773 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Properties of a Small Basic Peptide from Pumpkin Seeds 1

Gary H. Naisbitt, Mao-Rong Lu, William R. Gray and Leo P. Vernon

Chemistry Department, Brigham Young University, Provo, Utah 84602, Department of Biological Science and Biotechnology, Tsinghua University, Beijing, People's Republic of China, Biology Department, University of Utah, Salt Lake City, Utah 84112

A small basic peptide with an unusual amino acid composition has been isolated from the seeds of pumpkin, Cucurbita maxima. Amino acid analysis and sequence data show the protein to be about 36 residues in length, with an approximate composition Lys1, Arg14, Asp3, (Glu + Gln)15, Gly1, Pro1, Trp1. On the basis of composition, the molecular weight is approximately 5000 daltons and the nitrogen content by weight is 20.4%. Twelve amino acids are entirely lacking. The peptide is slightly toxic to mouse B-16 melanoma cells, but its in vivo function is unknown. It does not appear to be derived from cucurbitin, the pumpkin storage globulin; however, it could be a storage peptide involved in nitrogen mobilization during the early stages of germination.

1 This research was supported in part by research grants from Brigham Young University, the Bireley Foundation (LPV) and U.S. Public Health Service Biomedical Research Support grant RR 07092 to the University of Utah (W. R. G.).




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K. Yamada, T. Shimada, M. Kondo, M. Nishimura, and I. Hara-Nishimura
Multiple Functional Proteins Are Produced by Cleaving Asn-Gln Bonds of a Single Precursor by Vacuolar Processing Enzyme
J. Biol. Chem., January 22, 1999; 274(4): 2563 - 2570.
[Abstract] [Full Text] [PDF]


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Copyright © 1988 by the American Society of Plant Biologists