Purification Of Hydrogenase By Fast Protein Liquid Chromatography And By Conventional Separation Techniques

A Comparative Study

K. L. Kovacs, Gabor Tigyi

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Hydrogenase was purified from the photosynthetic bacterium Thiocapsa roseopersicina to homogeneity by various methods. Conventional techniques included separation of the crude protein extract on Phenyl-Sepharose CL 4B, DEAE-cellulose DE52, and chromatofocusing columns or on preparative polyacrylamide gelelectrophoresis. The same protein was isolated by fast protein liquid chromatography (FPLC) in two steps. Comparison of the two different approaches clearly show the superiority of the FPLC method both in enzyme recovery yield and in time requirement.

Original languageEnglish (US)
Pages (from-to)321-334
Number of pages14
JournalPreparative Biochemistry
Volume15
Issue number5
DOIs
StatePublished - Dec 1 1985

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Hydrogenase
Liquid chromatography
Liquid Chromatography
Purification
Thiocapsa roseopersicina
Proteins
DEAE-Cellulose
Complex Mixtures
Bacteria
Recovery
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Genetics

Cite this

Purification Of Hydrogenase By Fast Protein Liquid Chromatography And By Conventional Separation Techniques : A Comparative Study. / Kovacs, K. L.; Tigyi, Gabor.

In: Preparative Biochemistry, Vol. 15, No. 5, 01.12.1985, p. 321-334.

Research output: Contribution to journalArticle

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