TY - JOUR
T1 - Multiple molecular forms of insulin and glucagon-like peptide from the pacific ratfish (Hydrolagus colliei)
AU - Conlon, J. Michael
AU - Göke, Rüdiger
AU - Andrews, P. C.
AU - Thim, Lars
PY - 1989/1
Y1 - 1989/1
N2 - The primary structure of an insulin isolated from the pancreas of the holocephalan fish, Hydrolagus colliei (Pacific ratfish), has been established as {A figure is presented}. Three further molecular forms of insulin were also isolated and shown to have the same A-chain but truncated B-chains of 31-, 36-, and 37-amino acid residues. It is proposed that all four insulins arise from a single proinsulin by proteolytic cleavages at different sites within the C-peptide region. The insulin with 38 amino acids in the B-chain was equipotent with human insulin in inhibiting the binding of radiolabelled human insulin to rat fat cells but the maximum effect of ratfish insulin upon the transport of 3-O-methylglucose into the cells was only 65% of the maximum effect of human insulin. Two molecular forms of glucagon-like peptide were isolated from the ratfish pancreas. The primary structure of the more abundant peptide was established as {A figure is presented}. The primary structure of the second peptide was the same except that it was extended from the C-terminus by the sequence RRM. It is probable, therefore, that both glucagon-like peptides also arise from a single proglucagon by different pathways of post-translational processing.
AB - The primary structure of an insulin isolated from the pancreas of the holocephalan fish, Hydrolagus colliei (Pacific ratfish), has been established as {A figure is presented}. Three further molecular forms of insulin were also isolated and shown to have the same A-chain but truncated B-chains of 31-, 36-, and 37-amino acid residues. It is proposed that all four insulins arise from a single proinsulin by proteolytic cleavages at different sites within the C-peptide region. The insulin with 38 amino acids in the B-chain was equipotent with human insulin in inhibiting the binding of radiolabelled human insulin to rat fat cells but the maximum effect of ratfish insulin upon the transport of 3-O-methylglucose into the cells was only 65% of the maximum effect of human insulin. Two molecular forms of glucagon-like peptide were isolated from the ratfish pancreas. The primary structure of the more abundant peptide was established as {A figure is presented}. The primary structure of the second peptide was the same except that it was extended from the C-terminus by the sequence RRM. It is probable, therefore, that both glucagon-like peptides also arise from a single proglucagon by different pathways of post-translational processing.
UR - http://www.scopus.com/inward/record.url?scp=0024525848&partnerID=8YFLogxK
U2 - 10.1016/0016-6480(89)90064-6
DO - 10.1016/0016-6480(89)90064-6
M3 - Article
C2 - 2646172
AN - SCOPUS:0024525848
SN - 0016-6480
VL - 73
SP - 136
EP - 146
JO - General and Comparative Endocrinology
JF - General and Comparative Endocrinology
IS - 1
ER -