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Volumn 22, Issue 2, 2001, Pages 325-329

Rapid two-step purification of a recombinant mouse Fab fragment expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; BETA LACTAM; COAT PROTEIN; CONCENTRATION (PARAMETERS); HOMOGENIZATION; IMMUNOGLOBULIN F(AB) FRAGMENT; PH; PROTEIN INDUCTION; PROTEIN PURIFICATION; RECOMBINANT PROTEIN; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; SEPHAROSE; TOBACCO MOSAIC VIRUS;

EID: 0034963168     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1444     Document Type: Article
Times cited : (20)

References (19)
  • 3
    • 14744276972 scopus 로고
    • Antibody engineering: Advances from the use of Escherichia coli expression systems
    • (1991) Bio/Technology , vol.9 , pp. 545-551
    • Plückthun, A.1
  • 4
  • 9
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • (1997) Anal. Biochem. , vol.249 , pp. 153-164
    • Christensen, L.1
  • 13
    • 0024851846 scopus 로고
    • Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli
    • (1989) Gene , vol.85 , pp. 553-557
    • Cabilly, S.1
  • 15
    • 0033486375 scopus 로고    scopus 로고
    • Use of thiophilic adsorption chromatography for the one-step purification of a bacterially produced antibody Fab fragment without the need for an affinity tag
    • (1999) Protein Expression Purif. , vol.17 , pp. 421-427
    • Fiedler, M.1    Skerra, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.