Purification and structural characterization of insulin from a caecilian, Typhlonectes natans (Amphibia: Gymnophiona)

J. Michael Conlon; Caryl Hilscher-Conklin; Sunny K. Boyd

doi:10.1016/0196-9781(95)02033-0

Purification and structural characterization of insulin from a caecilian, Typhlonectes natans (Amphibia: Gymnophiona)

J. Michael Conlon
, Caryl Hilscher-Conklin
, Sunny K. Boyd

School of Biomedical Sciences

University of Notre Dame

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

14 Citations (Scopus)

Abstract

Despite the important position of amphibia in phylogeny, efforts at the structural characterization of amphibian neurohormonal peptides have largely been confined to the Anurans (frogs and toads). Insulin was purified from an extract of the pancreas of the caecilian, Typhlonectes natans. The primary structure of the peptide was established as: A-chain: Gly-Ile-Val-Glu-Lys⁵-Cys-Cys-Leu-Ser-Thr¹⁰-Cys-Ser-Leu-Tyr-Glu¹⁵-Leu-Glu-Ser-Tyr-Cys²⁰-Asn B-chain: Ile-Ala-Asn-Gln-His⁵-Leu-Cys-Gly-Ser-His¹⁰-Leu-Val-Glu-Ala-Leu¹⁵-Tyr-Leu-Val-Cys-Ala²⁰-Asp-Arg-Gly-Phe- Phe²⁵-Tyr-Thr-Pro-Lys-Ser³⁰. This amino acid sequence contains several unusual substitutions (Gln → Lys at A5, His → Leu at A8, Gln → Glu at A15, and Gly → Ala at B20) that are not present in other amphibian insulins. The structure of insulin appears to be less well conserved among the different orders of amphibia, compared with reptiles and birds.

Original language	English
Pages (from-to)	1385-1388
Number of pages	4
Journal	Peptides
Volume	16
Issue number	8
DOIs	https://doi.org/10.1016/0196-9781(95)02033-0
Publication status	Published (in print/issue) - 1995

Funding

This work was supported in part by NIH grant 9418819.

Funders	Funder number
National Institutes of Health	9418819
R29HD024653

Keywords

Amphibian
Caecilian
HPLC purification
Insulin

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title = "Purification and structural characterization of insulin from a caecilian, Typhlonectes natans (Amphibia: Gymnophiona)",

abstract = "Despite the important position of amphibia in phylogeny, efforts at the structural characterization of amphibian neurohormonal peptides have largely been confined to the Anurans (frogs and toads). Insulin was purified from an extract of the pancreas of the caecilian, Typhlonectes natans. The primary structure of the peptide was established as: A-chain: Gly-Ile-Val-Glu-Lys5-Cys-Cys-Leu-Ser-Thr10-Cys-Ser-Leu-Tyr-Glu15-Leu-Glu-Ser-Tyr-Cys20-Asn B-chain: Ile-Ala-Asn-Gln-His5-Leu-Cys-Gly-Ser-His10-Leu-Val-Glu-Ala-Leu15-Tyr-Leu-Val-Cys-Ala20-Asp-Arg-Gly-Phe- Phe25-Tyr-Thr-Pro-Lys-Ser30. This amino acid sequence contains several unusual substitutions (Gln → Lys at A5, His → Leu at A8, Gln → Glu at A15, and Gly → Ala at B20) that are not present in other amphibian insulins. The structure of insulin appears to be less well conserved among the different orders of amphibia, compared with reptiles and birds.",

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AU - Hilscher-Conklin, Caryl

AU - Boyd, Sunny K.

PY - 1995

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N2 - Despite the important position of amphibia in phylogeny, efforts at the structural characterization of amphibian neurohormonal peptides have largely been confined to the Anurans (frogs and toads). Insulin was purified from an extract of the pancreas of the caecilian, Typhlonectes natans. The primary structure of the peptide was established as: A-chain: Gly-Ile-Val-Glu-Lys5-Cys-Cys-Leu-Ser-Thr10-Cys-Ser-Leu-Tyr-Glu15-Leu-Glu-Ser-Tyr-Cys20-Asn B-chain: Ile-Ala-Asn-Gln-His5-Leu-Cys-Gly-Ser-His10-Leu-Val-Glu-Ala-Leu15-Tyr-Leu-Val-Cys-Ala20-Asp-Arg-Gly-Phe- Phe25-Tyr-Thr-Pro-Lys-Ser30. This amino acid sequence contains several unusual substitutions (Gln → Lys at A5, His → Leu at A8, Gln → Glu at A15, and Gly → Ala at B20) that are not present in other amphibian insulins. The structure of insulin appears to be less well conserved among the different orders of amphibia, compared with reptiles and birds.

AB - Despite the important position of amphibia in phylogeny, efforts at the structural characterization of amphibian neurohormonal peptides have largely been confined to the Anurans (frogs and toads). Insulin was purified from an extract of the pancreas of the caecilian, Typhlonectes natans. The primary structure of the peptide was established as: A-chain: Gly-Ile-Val-Glu-Lys5-Cys-Cys-Leu-Ser-Thr10-Cys-Ser-Leu-Tyr-Glu15-Leu-Glu-Ser-Tyr-Cys20-Asn B-chain: Ile-Ala-Asn-Gln-His5-Leu-Cys-Gly-Ser-His10-Leu-Val-Glu-Ala-Leu15-Tyr-Leu-Val-Cys-Ala20-Asp-Arg-Gly-Phe- Phe25-Tyr-Thr-Pro-Lys-Ser30. This amino acid sequence contains several unusual substitutions (Gln → Lys at A5, His → Leu at A8, Gln → Glu at A15, and Gly → Ala at B20) that are not present in other amphibian insulins. The structure of insulin appears to be less well conserved among the different orders of amphibia, compared with reptiles and birds.

KW - Amphibian

KW - Caecilian

KW - HPLC purification

KW - Insulin

UR - https://www.scopus.com/pages/publications/0028886105

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DO - 10.1016/0196-9781(95)02033-0

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JF - Peptides

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ER -

Purification and structural characterization of insulin from a caecilian, Typhlonectes natans (Amphibia: Gymnophiona)

Abstract

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Keywords

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