title: Production and purification of recombinant human glucagon overexpressed as intein fusion protein in Escherichia coli.
abstract: Chemico-enzymatic synthesis and cloning in Esherichia coli of an artificial gene coding human glucagon was performed. Recombinant plasmid containing hybrid glucagons gene and intein Ssp dnaB from Synechocestis sp. was designed. Expression of the obtained hybrid gene in E. coli, properties of the formed hybrid protein, and conditions of its autocatalytic cleavage leading to glucagon formation were studied.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia. esipov@ibch.ru
authors.forename: Roman S
authors.initials: RS
authors.lastname: Esipov
authors.forename: Vasily N
authors.initials: VN
authors.lastname: Stepanenko
authors.forename: Alexandr I
authors.initials: AI
authors.lastname: Gurevich
authors.forename: Larisa A
authors.initials: LA
authors.lastname: Chupova
authors.forename: Anatoly I
authors.initials: AI
authors.lastname: Miroshnikov
mesh_terms: D000595:Amino Acid Sequence; D004586:Electrophoresis; D004926:Escherichia coli / Q000378:metabolism; D005934:Glucagon / Q000096:biosynthesis*; D006801:Humans; D047668:Inteins / Q000235:genetics; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000302:isolation & purification
chemical_list: D011993:Recombinant Fusion Proteins; D005934:Glucagon