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Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini

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Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. / Anderson, W G ; Ali, M F ; Einarsdottir, I E ; Schaffer, L ; Hazon, N ; Conlon, J M .

In: General and Comparative Endocrinology, Vol. 126, 03.2002, p. 113-122.

Research output: Contribution to journalArticle

Harvard

Anderson, WG, Ali, MF, Einarsdottir, IE, Schaffer, L, Hazon, N & Conlon, JM 2002, 'Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini' General and Comparative Endocrinology, vol. 126, pp. 113-122. https://doi.org/10.1006/gcen.2002.7787

APA

Anderson, W. G., Ali, M. F., Einarsdottir, I. E., Schaffer, L., Hazon, N., & Conlon, J. M. (2002). Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. General and Comparative Endocrinology, 126, 113-122. https://doi.org/10.1006/gcen.2002.7787

Vancouver

Anderson WG, Ali MF, Einarsdottir IE, Schaffer L, Hazon N, Conlon JM. Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. General and Comparative Endocrinology. 2002 Mar;126:113-122. https://doi.org/10.1006/gcen.2002.7787

Author

Anderson, W G ; Ali, M F ; Einarsdottir, I E ; Schaffer, L ; Hazon, N ; Conlon, J M . / Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. In: General and Comparative Endocrinology. 2002 ; Vol. 126. pp. 113-122.

Bibtex - Download

@article{bcf4536451904722a8807f9f7dfbc9a0,
title = "Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini",
abstract = "Insulin was purified from pancreatic extracts of two elasmobranch species belonging to different families in the order Carcharhiniformes, the European spotted dogfish, Scyliorhinus canicula (Scyliorhinidae), and the hammerhead shark, Sphyrna lewini (Carcharhinidae). The amino acid sequence of dogfish insulin was established as A-chain GIVDHCCRNT(10) CSLYDLEGYC(20)NQ and B-chain LPSQHLCGSH(10)LVETLYFVCG(20)QKGFYYVPKV(30). The primary structure of hammerhead shark insulin was similar to that of dogfish insulin with only 2 amino acid substitutions at A8 (R --> H) and B30 (V --> I). The elasmobranch insulins were markedly different from human insulin (17 amino acid substitutions) but all the residues in human insulin that are believed to be important in determining the receptor binding conformation (B6, B8, B11, B13, B23, B24, B25, A2, A3, and A19) have been conserved in the elasmobranch insulins with the exception of the conservative substitution Phe --> Tyr at B25. Consistent with this, dogfish and human insulin showed almost identical binding affinity to the recombinant solubilized human insulin receptor (K-D values of 14.0 and 18.6 pM, respectively; relative potency 133{\%}). Previous studies have shown that bovine insulin produces severe and sustained hypoglycemia in elasmobranchs but the effect is of slow onset. Bolus arterial injections of dogfish insulin (10 nmol (.) kg(-1)) into unanesthetized, fasting dogfish (n = 9) produced no changes in blood glucose, 3-hydroxybutyrate, and acetoacetate concentrations over a 4-h period. In a second series of experiments (n = 7), dogfish insulin (10 nmol (.) kg(-1)) produced a significant (P < 0.05) fall in blood glucose after 12 h that persisted for at least 48 h, but no change in ketone body concentrations. The data indicate that the metabolic actions of an endogenous elasmobranch insulin in an elasmobranch are similar to those previously described for mammalian insulin. (C) 2002 Elsevier Science (USA).",
keywords = "insulin purification, elasmobranch, insulin receptor, glucose, acetoacetate, 3-hydroxybutyrate, STRUCTURAL CHARACTERIZATION, RECEPTOR-BINDING, GLUCOSE, FISH, PEPTIDE, GLUCAGON, MOLECULE, INSIGHTS, PANCREAS, ALANINE",
author = "Anderson, {W G} and Ali, {M F} and Einarsdottir, {I E} and L Schaffer and N Hazon and Conlon, {J M}",
year = "2002",
month = "3",
doi = "10.1006/gcen.2002.7787",
language = "English",
volume = "126",
pages = "113--122",
journal = "General and Comparative Endocrinology",
issn = "0016-6480",
publisher = "Academic Press Inc.",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini

AU - Anderson, W G

AU - Ali, M F

AU - Einarsdottir, I E

AU - Schaffer, L

AU - Hazon, N

AU - Conlon, J M

PY - 2002/3

Y1 - 2002/3

N2 - Insulin was purified from pancreatic extracts of two elasmobranch species belonging to different families in the order Carcharhiniformes, the European spotted dogfish, Scyliorhinus canicula (Scyliorhinidae), and the hammerhead shark, Sphyrna lewini (Carcharhinidae). The amino acid sequence of dogfish insulin was established as A-chain GIVDHCCRNT(10) CSLYDLEGYC(20)NQ and B-chain LPSQHLCGSH(10)LVETLYFVCG(20)QKGFYYVPKV(30). The primary structure of hammerhead shark insulin was similar to that of dogfish insulin with only 2 amino acid substitutions at A8 (R --> H) and B30 (V --> I). The elasmobranch insulins were markedly different from human insulin (17 amino acid substitutions) but all the residues in human insulin that are believed to be important in determining the receptor binding conformation (B6, B8, B11, B13, B23, B24, B25, A2, A3, and A19) have been conserved in the elasmobranch insulins with the exception of the conservative substitution Phe --> Tyr at B25. Consistent with this, dogfish and human insulin showed almost identical binding affinity to the recombinant solubilized human insulin receptor (K-D values of 14.0 and 18.6 pM, respectively; relative potency 133%). Previous studies have shown that bovine insulin produces severe and sustained hypoglycemia in elasmobranchs but the effect is of slow onset. Bolus arterial injections of dogfish insulin (10 nmol (.) kg(-1)) into unanesthetized, fasting dogfish (n = 9) produced no changes in blood glucose, 3-hydroxybutyrate, and acetoacetate concentrations over a 4-h period. In a second series of experiments (n = 7), dogfish insulin (10 nmol (.) kg(-1)) produced a significant (P < 0.05) fall in blood glucose after 12 h that persisted for at least 48 h, but no change in ketone body concentrations. The data indicate that the metabolic actions of an endogenous elasmobranch insulin in an elasmobranch are similar to those previously described for mammalian insulin. (C) 2002 Elsevier Science (USA).

AB - Insulin was purified from pancreatic extracts of two elasmobranch species belonging to different families in the order Carcharhiniformes, the European spotted dogfish, Scyliorhinus canicula (Scyliorhinidae), and the hammerhead shark, Sphyrna lewini (Carcharhinidae). The amino acid sequence of dogfish insulin was established as A-chain GIVDHCCRNT(10) CSLYDLEGYC(20)NQ and B-chain LPSQHLCGSH(10)LVETLYFVCG(20)QKGFYYVPKV(30). The primary structure of hammerhead shark insulin was similar to that of dogfish insulin with only 2 amino acid substitutions at A8 (R --> H) and B30 (V --> I). The elasmobranch insulins were markedly different from human insulin (17 amino acid substitutions) but all the residues in human insulin that are believed to be important in determining the receptor binding conformation (B6, B8, B11, B13, B23, B24, B25, A2, A3, and A19) have been conserved in the elasmobranch insulins with the exception of the conservative substitution Phe --> Tyr at B25. Consistent with this, dogfish and human insulin showed almost identical binding affinity to the recombinant solubilized human insulin receptor (K-D values of 14.0 and 18.6 pM, respectively; relative potency 133%). Previous studies have shown that bovine insulin produces severe and sustained hypoglycemia in elasmobranchs but the effect is of slow onset. Bolus arterial injections of dogfish insulin (10 nmol (.) kg(-1)) into unanesthetized, fasting dogfish (n = 9) produced no changes in blood glucose, 3-hydroxybutyrate, and acetoacetate concentrations over a 4-h period. In a second series of experiments (n = 7), dogfish insulin (10 nmol (.) kg(-1)) produced a significant (P < 0.05) fall in blood glucose after 12 h that persisted for at least 48 h, but no change in ketone body concentrations. The data indicate that the metabolic actions of an endogenous elasmobranch insulin in an elasmobranch are similar to those previously described for mammalian insulin. (C) 2002 Elsevier Science (USA).

KW - insulin purification

KW - elasmobranch

KW - insulin receptor

KW - glucose

KW - acetoacetate

KW - 3-hydroxybutyrate

KW - STRUCTURAL CHARACTERIZATION

KW - RECEPTOR-BINDING

KW - GLUCOSE

KW - FISH

KW - PEPTIDE

KW - GLUCAGON

KW - MOLECULE

KW - INSIGHTS

KW - PANCREAS

KW - ALANINE

UR - http://www.scopus.com/inward/record.url?scp=0036232442&partnerID=8YFLogxK

U2 - 10.1006/gcen.2002.7787

DO - 10.1006/gcen.2002.7787

M3 - Article

VL - 126

SP - 113

EP - 122

JO - General and Comparative Endocrinology

T2 - General and Comparative Endocrinology

JF - General and Comparative Endocrinology

SN - 0016-6480

ER -

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ID: 778600