Identification and Partial Purification of Two Hydrogenase Isoenzymes from Escherichia coli

대장균으로부터 두 종류의 수소발생 동위효소의 확인과 부분정제

  • 최석정 (강릉대학교 화학과) ;
  • 양철학 (서울대학교 화학과)
  • Published : 1991.11.01


The membrane-bound Escherichia coli hydrogenases were purified partially by the solubilization with detergents. the E. coli crude extract was solubilized with sodium deoxycholate and dialyzed against the buffer containing Triton X-100. Two different hydrogenases were obtained by the DEAE-cellulose, hydroxyapatite and Sephedex G-200 column chromatography. The one was unstable during purification and contained 70- and 47-kDa polypeptides as major proteins. The other showed high H2-evolving activity and had major polypeptides of Mr 31 and 27. Those polypeptides were detected by the two-dimensional electrophoresis.


Escherichia coli;hydrogenase isoenzymes;sodium deoxycholate;Triton X-100