遺伝子組換え型シロザケ成長ホルモンの諸性質〔英文〕

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We have characterized and purified recombinant salmon growth hormone I (rSGH I). The primary structure of rSGH I confirmed by N-terminal sequence analysis, amino acid composition analysis, and tryptic and thermolytic mapping was identical to that deduced from SGH I com-plementary deoxyribonucleic acid except for an additional Met at N-terminal. Peptide mapping also revealed that rSGH I had two disulfide bonds, Cys49-Cys161 and Cys178-Cys186, as in mam-malian GHs. Recombinant SGH I, as well as natural SGH I, was classified as an alpha-helix rich protein from its circular dichroism spectrum. Recombinant SGH I was equipotent with natural SGH I in receptor binding assay. Gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that rSGH I exists as a monomer like natural SGH I.
日本水産學會の論文