TY - JOUR
T1 - The primary structure of Glucagon-like peptide but not insulin has been conserved between the American eel, Anguilla rostrata and the European eel, Anguilla anguilla
AU - Conlon, J. Michael
AU - Andrews, P. C.
AU - Thim, Lars
AU - Moon, Thomas W.
N1 - Funding Information:
This work was supported by the Natural Sciences and Engineering Council of Canada and by the Ontario Ministry of Natural Resources. Dr. P. C. Andrews was supported in part by a research and development award from the American Diabetes Association. The authors wish to thank Mr. Cl. Foster, University of Ottawa, Canada, and Dr. N. Hazon, University of St. Andrews, U.K., for help in tissue collection.
PY - 1991/4
Y1 - 1991/4
N2 - Insulin was isolated from the pancreas of the American eel, Anguilla rostrata, and its primary structure was established as {A figure is presented} Eel insulin contains unusual substitutions at B-21, B-22, and B-26 in the putative receptor-binding region of the molecule compared with other mammalian and fish insulins. The A-chain of insulin from the European eel contains an asparagine rather than a serine residue at position A-12. Similarly, amino acid composition data indicate the B-chain of insulin from the European eel is appreciably different from that from the American eel. The primary structure of glucagon-like peptide (GLP) from the American eel is identical to that from the European eel, Anguilla anguilla. The primary structure of the peptide was established as {A figure is presented} Fast-atom bombardment mass spectrometry demonstrated that the COOH-terminal arginyl residue is α-amidated. The strong evolutionary pressure to conserve the structure of GLP provides further support for the assertion that the peptide plays an important regulatory role in teleost fish.
AB - Insulin was isolated from the pancreas of the American eel, Anguilla rostrata, and its primary structure was established as {A figure is presented} Eel insulin contains unusual substitutions at B-21, B-22, and B-26 in the putative receptor-binding region of the molecule compared with other mammalian and fish insulins. The A-chain of insulin from the European eel contains an asparagine rather than a serine residue at position A-12. Similarly, amino acid composition data indicate the B-chain of insulin from the European eel is appreciably different from that from the American eel. The primary structure of glucagon-like peptide (GLP) from the American eel is identical to that from the European eel, Anguilla anguilla. The primary structure of the peptide was established as {A figure is presented} Fast-atom bombardment mass spectrometry demonstrated that the COOH-terminal arginyl residue is α-amidated. The strong evolutionary pressure to conserve the structure of GLP provides further support for the assertion that the peptide plays an important regulatory role in teleost fish.
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U2 - 10.1016/0016-6480(91)90292-E
DO - 10.1016/0016-6480(91)90292-E
M3 - Article
C2 - 1874385
AN - SCOPUS:0025727052
SN - 0016-6480
VL - 82
SP - 23
EP - 32
JO - General and Comparative Endocrinology
JF - General and Comparative Endocrinology
IS - 1
ER -