Porcine Proinsulin: Characterization and Amino Acid Sequence

Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalan...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1968-07, Vol.161 (3837), p.165-167
Hauptverfasser:	Chance, Ronald E., Ellis, Robert M., Bromer, William W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Animals Biological Assay Cellulose Chickens Chromatography Chromatography, Ion Exchange Chymotrypsin Electrophoresis Electrophoresis, Disc Enzymes Gels Hypoglycemia - chemically induced Insulin Molecular Weight Peptides - analysis Polydipsia Polyuria Proteins - analysis Seizures - chemically induced Swine Teeth Trypsin
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Beschreibung
Zusammenfassung:	Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly - Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.161.3837.165