Open AccessProperties of a Small Basic Peptide from Pumpkin Seeds
Author(s) -
Gary H. Naisbitt,
Mao-Rong Lu,
William R. Gray,
Leo P. Ver
Publication year - 1988
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.88.3.770
Subject(s) - cucurbita maxima , peptide , amino acid , composition (language) , germination , storage protein , peptide sequence , cucurbita , chemistry , biology , biochemistry , pumpkin seed , botany , food science , linguistics , philosophy , gene
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 Lys(1), Arg(14), Asp(3), (Glu + Gln)(15), Gly(1), Pro(1), Trp(1). 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.