Insulin-Stimulating Peptide from a Tryptic Digest of Bovine Serum Albumin: Purification and Characterization1

Autor:	Yeong-Man Hong, Naokatu Arakaki, Yoshiro Takeda, Akemichi Ueno
Rok vydání:	1985
Předmět:	chemistry.chemical_classification Chromatography biology Chemistry Ion chromatography Size-exclusion chromatography Serum albumin Albumin Peptide General Medicine Biochemistry High-performance liquid chromatography Column chromatography biology.protein Bovine serum albumin Molecular Biology
Zdroj:	The Journal of Biochemistry. 98:269-278
ISSN:	1756-2651 0021-924X
DOI:	10.1093/oxfordjournals.jbchem.a135280
Popis:	A procedure was established for isolation of a low molecular weight polypeptide with insulin-stimulating activity in apparent homogeneity from a tryptic digest of bovine serum albumin on a semipreparative scale. Purification of this insulin-stimulating peptide (ISP) was monitored by an adipose-explant assay in which stimulation of fatty acid synthesis from glucose by insulin was measured. The polypeptide was purified by a combination of DEAE-cellulose column chromatography, gel filtration on Bio-Gel P-10, hydrophobic chromatography on a semipreparative C18 reversed-phase HPLC column, and ion exchange chromatography on an SP-5PW HPLC column. The primary structure of ISP was deduced. ISP is a two-chain polypeptide consisting of 71 amino acid residues, and corresponds essentially to residues 115-143 and 144-184 (185) of bovine serum albumin connected to each other by a disulfide bridge. But comparison of the sequence of ISP with that of the relevant regions of bovine serum albumin determined by Brown indicated the presence of one tyrosine insertion between residues 155 and 156 of albumin. Therefore, the molecular weight of ISP was calculated to be 8,496.
Databáze:	OpenAIRE
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