메뉴 건너뛰기




Volumn 73, Issue 6, 2001, Pages 484-492

DegP-coexpression minimizes inclusion-body formation upon overproduction of recombinant penicillin acylase in Escherichia coli

Author keywords

DegP; Escherichia coli; Inclusion body; Penicillin acylase; Periplasm; Protease; Proteolysis

Indexed keywords

ENZYMES; ESCHERICHIA COLI; GENES;

EID: 0035919127     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.1083     Document Type: Article
Times cited : (24)

References (40)
  • 4
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • (1992) Anal Biochem , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 12
  • 19
    • 0025955658 scopus 로고
    • Refolding and assembly of penicillin acylase, an enzyme composed of two polypeptide chains that result from proteolytic activation
    • (1991) Biochemistry-USA , vol.30 , pp. 9034-9040
    • Lindsay, C.D.1    Pain, R.H.2
  • 20
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • (1996) Microbiol Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 21
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins
    • (1994) Bio/Technology , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgoiu, G.2
  • 35
  • 40


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.