ISOLATION AND STRUCTURAL CHARACTERIZATION OF INSULIN AND GLUCAGON FROM THE HOLOCEPHALAN SPECIES CALLORHYNCHUS-MILII (ELEPHANTFISH)
ISOLATION AND STRUCTURAL CHARACTERIZATION OF INSULIN AND GLUCAGON FROM THE HOLOCEPHALAN SPECIES CALLORHYNCHUS-MILII (ELEPHANTFISH)
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DOI:
10.1042/bj2630261
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发表时间:
1989-10-01
影响因子:
4.1
通讯作者:
CUTFIELD, JF
中科院分区:
文献类型:
--
作者:
BERKS, BC;MARSHALL, CJ;CUTFIELD, JF
Both insulin and glucagon from the pancreas of the holocephalan cartilaginous fish Callorhynchus milii (elephantfish) have been isolated and purified. Two reverse-phase h.p.l.c. steps enabled recovery of sufficient material for gas-phase sequencing of the intact chains as well as peptide digestion products. The elephantfish insulin sequence shows 14 differences from pig insulin, including two unusual substitutions. The insulin B-chain contains 31 residues, one more than mammalian insulins, but markedly less than that of the closely related ratfish with which it otherwise exhibits high sequence similarity. Elephantfish and pig glucagons differ at only four positions, but there are six changes from the ratfish glucagon-36 (normal glucagon contains 29 residues) sequence. It is apparent that different prohormone proteolytic processing mechanisms operate in the two holocephalan species.