Amino acid sequence of growth hormone isolated from medium of incubated pituitary glands of tilapia (Oreochromis mossambicus)
Document Type
Article
Date of Original Version
1-1-1991
Abstract
The amino acid sequence of tilapia (Oreochromis mossambicus) growth hormone (GH) was determined directly by Edman degradation of peptide fragments generated by lysyl endopeptidase and trypsin digestion. The N-terminal residue was deduced to be pyroglutamic acid through the use of pyroglutamyl aminopeptidase; its removal allowed amino acid sequence determination of the remainder of the N-terminal trypsin peptide by Edman degradation. Tilapia GH is composed of 187 amino acid residues and shows high similarity to other perciform GHs. Sequence identities are: 89% with tuna GH, 83% with bonito GH, 85% with yellowtail GH, 89% with red sea bream GH, and 34% with bovine GH. The two asparagine residues (Asn-148 and Asn-184) were recovered by Edman degradation, suggesting the absence of N-glycosylation. © 1991.
Publication Title, e.g., Journal
General and Comparative Endocrinology
Volume
81
Issue
2
Citation/Publisher Attribution
Yamaguchi, Kazuo, David S. King, Jennifer L. Specker, Richard S. Nishioka, Tetsuya Hirano, and Howard A. Bern. "Amino acid sequence of growth hormone isolated from medium of incubated pituitary glands of tilapia (Oreochromis mossambicus)." General and Comparative Endocrinology 81, 2 (1991). doi: 10.1016/0016-6480(91)90017-Z.
