title: A new approach to characterization of insulin derived from different species using 1H-NMR coupled with multivariate analysis.
abstract: Most of the active components of polypeptides have a complex molecular structure, large molecular size. Such components may also be structurally heterogeneous. Therefore, development of a method that can confirm the consistency of polypeptides amino-acid sequences for product characterization is desirable. In general, it is extremely difficult to distinguish differences of a few amino acid residues in the 1H-NMR spectrum of polypeptides with molecular weights greater than several thousand. However, we have been able to distinguish between three insulin species differing in one to three amino acid residues using a combination of multivariate statistics and 1H-NMR spectra. These results demonstrate that this methodology could be useful for characterization of polypeptides.
authors.affiliation: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan. ako-ohno@nihs.go.jp
authors.forename: Akiko
authors.initials: A
authors.lastname: Ohno
authors.forename: Toru
authors.initials: T
authors.lastname: Kawanishi
authors.forename: Haruhiro
authors.initials: H
authors.lastname: Okuda
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Fukuhara
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002417:Cattle; D006801:Humans; D007328:Insulin / Q000737:chemistry*; D008279:Magnetic Resonance Imaging / Q000379:methods; D008969:Molecular Sequence Data; D015394:Molecular Structure; D008970:Molecular Weight; D015999:Multivariate Analysis; D010455:Peptides / Q000737:chemistry; D013552:Swine
chemical_list: D000596:Amino Acids; D007328:Insulin; D010455:Peptides