TY - JOUR
T1 - Purification and structural characterization of insulin from a caecilian, Typhlonectes natans (Amphibia: Gymnophiona)
AU - Conlon, J. Michael
AU - Hilscher-Conklin, Caryl
AU - Boyd, Sunny K.
PY - 1995
Y1 - 1995
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 - http://www.scopus.com/inward/record.url?scp=0028886105&partnerID=8YFLogxK
U2 - 10.1016/0196-9781(95)02033-0
DO - 10.1016/0196-9781(95)02033-0
M3 - Article
C2 - 8745047
AN - SCOPUS:0028886105
SN - 0196-9781
VL - 16
SP - 1385
EP - 1388
JO - Peptides
JF - Peptides
IS - 8
ER -