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Titolo:
Secretion expression of recombinant glucagon in Escherichia coli
Autore:
Wen, CW; Wang, ZR; Du, P; Gan, RB; Zhu, SQ;
Indirizzi:
Chinese Acad Sci, Shanghai Inst Biochem, Shanghai 200031, Peoples R China Chinese Acad Sci Shanghai Peoples R China 200031 200031, Peoples R China
Titolo Testata:
SCIENCE IN CHINA SERIES C-LIFE SCIENCES
fascicolo: 3, volume: 44, anno: 2001,
pagine: 233 - 240
SICI:
1006-9305(200106)44:3<233:SEORGI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
REPLACEMENT ANALOGS; CHARGED RESIDUES; SIGNAL SEQUENCE; FUSION PROTEIN; PATHOGENESIS; POSITION-17; BINDING; TRYPSIN; HORMONE; REGION;
Keywords:
glucagon; phoA expression system; secretion;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Gan, RB Chinese Acad Sci, Shanghai Inst Biochem, Shanghai 200031, Peoples R China Chinese Acad Sci Shanghai Peoples R China 200031 Peoples R China
Citazione:
C.W. Wen et al., "Secretion expression of recombinant glucagon in Escherichia coli", SCI CHINA C, 44(3), 2001, pp. 233-240

Abstract

A novel approach for the preparation of recombinant human glucagon was described. An expression vector pAGluT, containing phoA promoter, phoA signal peptide and glucagon gene, was constructed by means of genetic engineering. Escherichia coli strain YK537 was transformed with pAGluT. High-level secretory expression of recombinant human glucagon was achieved. The expressionyield of recombinant human glucagon was found to be 80 mg/L, approximately30% of the total proteins in supernatant. The biological activities and the physicochemical properties of the purified recombinant human glucagon were found to be the same as that of native glucagon. In addition, our resultssuggested that phoA expression system may be suitable for the expression of other small peptides.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 12:48:31