Amino acid sequence of growth hormone isolated from medium of incubated pituitary glands of tilapia (Oreochromis mossambicus)

Authors

Kazuo Yamaguchi, Kyowa Kirin Co., Ltd.
David S. King, University of California, Berkeley
Jennifer L. Specker, University of Rhode Island
Richard S. Nishioka, University of California, Berkeley
Tetsuya Hirano, University of California, Berkeley
Howard A. Bern, University of California, Berkeley

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.