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Titolo:
A large-scale purification of recombinant histone H1.5 from Escherichia coli
Autore:
Pyo, SH; Lee, JH; Park, HB; Hong, SS; Kim, JH;
Indirizzi:
Kongju Natl Univ, Dept Chem Engn, Kong Ju 314701, Chungnam, South Korea Kongju Natl Univ Kong Ju Chungnam South Korea 314701 hungnam, South Korea Samyant Genex Biotech Res Inst, Taejon 305348, South Korea Samyant Genex Biotech Res Inst Taejon South Korea 305348 48, South Korea
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 1, volume: 23, anno: 2001,
pagine: 38 - 44
SICI:
1046-5928(200110)23:1<38:ALPORH>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Kim, JH Kongju Natl Univ, Dept Chem Engn, 182 Shinkwan Dong, Kong Ju 314701, Chungnam, South Korea Kongju Natl Univ 182 Shinkwan Dong Kong Ju Chungnam South Korea 314701
Citazione:
S.H. Pyo et al., "A large-scale purification of recombinant histone H1.5 from Escherichia coli", PROT EX PUR, 23(1), 2001, pp. 38-44

Abstract

An Escherichia coli expression system has been constructed for production of biologically active recombinant histone H1.5. A process of fermentation and purification method at a large scale has been developed. Recombinant histone H1.5 was released from the high density cultured cells by high-pressure homogenization. For an efficient removal of cell debris and partial purification of basic histone H1.5 in a single step, the whole cell lysates were directly loaded onto an expanded bed column packed with the strong cationexchanger (Streamline SP). Complete removal of various impurities was achieved by a combination of hydroxyapatite chromatography and the following cation exchange chromatography with high grade strong cation exchanger (POROS20 HS), and finally endotoxins were removed by ultrafiltration using a 100-kDa cut-off membrane, which gave the level of endotoxin below 0.5 EU/mg. The molecular mass of the recombinant histone H1.5 analyzed by MALDI-TOFMS, and the N-terminal amino acid sequences were in good agreement with the authentic histone H1.5. The whole process gave highly purified recombinant histone H1.5 at a high yield, compared to the conventional process. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 00:22:46