Isolation and structural characterization of insulin from the holocephalan fish, Chimaera monstrosa (rabbit fish)

J. Michael Conlon; P. C. Andrews; Sture Falkmer; Lars Thima

doi:10.1016/0016-6480(88)90191-8

Isolation and structural characterization of insulin from the holocephalan fish, Chimaera monstrosa (rabbit fish)

J. Michael Conlon
, P. C. Andrews
, Sture Falkmer
, Lars Thima

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

Insulin has been isolated from the pancreas of the holocephalan fish, Chimaera monstrosa (rabbit fish), and characterized by automated Edman degradation and fast atom bombardment mass spectrometry. The primary structure of rabbit fish insulin was identical to that of insulin from the holocephalan fish, Hydrolagus colliei (Pacific ratfish), and contained 21 residues in the A-chain and 38 residues in the B-chain. The amino acid compositions of both rabbit fish and ratfish insulins demonstrated a value consistently lower than that expected for the leucine content of the peptides. It is suggested, therefore, that the insulins were probably isolated as a mixture of the intact peptides and components lacking the C-terminal leucine residue in the B-chain.

Original language	English
Pages (from-to)	154-160
Number of pages	7
Journal	General and Comparative Endocrinology
Volume	72
Issue number	1
DOIs	https://doi.org/10.1016/0016-6480(88)90191-8
Publication status	Published (in print/issue) - Oct 1988

Funding

The authors thank the Stiftung Volkswagenwerk, the Swedish Medical Research Council (12X-718), the Swedish Diabetes Association, and the Cancer Society of Stockholm for financial support; and Professor N. Hilschmann, Max-Planck-Institut fur Experimentelle Medizin, Gottingen, for providing facilities for amino acid analysis. Dr. P. C. Andrews was supported in part by a research and development award from the American Diabetes Association. Thanks are due to the director and staff of the Marine Biology Station, University of Bergen, Norway.

Funders	Funder number
Max-Planck-Institut fur Experimentelle Medizin
12X-718

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AU - Thima, Lars

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AB - Insulin has been isolated from the pancreas of the holocephalan fish, Chimaera monstrosa (rabbit fish), and characterized by automated Edman degradation and fast atom bombardment mass spectrometry. The primary structure of rabbit fish insulin was identical to that of insulin from the holocephalan fish, Hydrolagus colliei (Pacific ratfish), and contained 21 residues in the A-chain and 38 residues in the B-chain. The amino acid compositions of both rabbit fish and ratfish insulins demonstrated a value consistently lower than that expected for the leucine content of the peptides. It is suggested, therefore, that the insulins were probably isolated as a mixture of the intact peptides and components lacking the C-terminal leucine residue in the B-chain.

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Isolation and structural characterization of insulin from the holocephalan fish, Chimaera monstrosa (rabbit fish)

Abstract

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