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- W2081862219 abstract "Abstract The characterization of purified recombinant eel growth hormone (rEGH) is described. N-Terminal sequence analysis, amino acid composition analysis, and tryptic mapping confirmed that the primary structure of rEGH was identical with that of its natural counterpart except for an additional Met at the N-terminus. Peptide mapping also revealed that rEGH had two disulphide bonds, Cys49-Cysl6O and Cysl77-Cysl85, as in mammalian growth hormones (GHs). Recombinant EGH was classified as an α-helix-rich protein, similar to mammalian GHs, from the circular dichroism spectrum. Recombinant EGH was immunochemically identical with pituitary-derived EGH. Gel filtration chromatography and light-scattering analysis indicated that rEGH exists as the monomer, as does pituitary-derived EGH." @default.
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- W2081862219 date "1991-06-01" @default.
- W2081862219 modified "2023-09-27" @default.
- W2081862219 title "Characterization of recombinant eel growth hormone" @default.
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- W2081862219 doi "https://doi.org/10.1016/s0021-9673(01)88636-2" @default.
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