title: [Analytical biotechnology of recombinant peptides and proteins. I. Analysis of the purity, composition and structure of human, porcine and bovine insulins].
abstract: A method for analysis of the type, purity, and possible structural modifications of insulins of bovine, porcine, and human origin was proposed. It is based on a combination of narrow-bore reversed-phase HPLC and mass spectrometry. The hydrolysis of insulins with highly specific Glu-protease V8 from Staphylococcus aureus followed by peptide mapping of the hydrolysis products and mass spectrometry of the isolated fragments helps rapidly and reliably localize and identify substitutions of amino acid residues in insulin structure by using insulin samples of less than 1 nmol.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. nazimov@ibch.siobc.ras.ru
authors.forename: N V
authors.initials: NV
authors.lastname: Sergeev
authors.forename: I V
authors.initials: IV
authors.lastname: Nazimov
authors.forename: V G
authors.initials: VG
authors.lastname: Gavrikov
authors.forename: A I
authors.initials: AI
authors.lastname: Miroshnikov
mesh_terms: D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007328:Insulin / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D013058:Mass Spectrometry; D011994:Recombinant Proteins / Q000032:analysis / Q000737:chemistry; D013552:Swine
chemical_list: D007328:Insulin; D011994:Recombinant Proteins