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Lee, Jehee,Munasinghe, Helani,Song, Choon Bok 한국수산학회 2003 Fisheries and Aquatic Sciences Vol.6 No.3
Isolation and cloning of seven-band grouper (Epirzephelus septenzfusciatus) growth hormone cDNA from pituitary gland revealed an open reading frame of 612 bp coding for a pre-growth hormone of 204 amino acids with a 17 amino acid putative signal peptide. Deduced amino acid sequence showed that there was one ossible N-glycosylation site at Asn^(184) and four cysteine residues (Cys^(52), Cys^(160), Cys^(177), Cys^(185) on the same positions as in some other species where they were involved in the stabilization of the tertiary structure. The seven-band grouper growth hormone (sbgGH) presented a 99.5% amino acid sequence identity with the growth hormone of Epinephelus coioides and contained the conserved hormone domain region. Comparison of growth hormone sequences from evolutionarily diverse species revealed 25 amino acid residues conserved in jawless fishes to modern mammals. It also revealed an evolutionary trend to retain the same polypeptide sequence even in the distantly related animals while allowing alterations to occur in polypeptides of the closely related species. In order to create a recombinant system to produce high levels of the growth hormone, it was expressed in Escherichia coli (BL21) cells. The gel analysis revealed theoretically expected molecular weights for both mature and pre-sbgGHs.