@article{oai:kanazawa-u.repo.nii.ac.jp:00053793,
 author = {板垣, 英治 and Fujita, Takeshi and Itagaki, Eiji and Sato, Ryo},
 issue = {4},
 journal = {The Journal of Biochemistry},
 month = {},
 note = {Cytochrome b1 was solubilized from the particulate fraction of Escherichia coli with the aid of snake venom and deoxycholate and was extensively purified by ammonium sul-fate fractionation and hydroxylapatite column chromatography. The purifed preparation was still contaminated by a colorless impurity which sedimented more slowly than the cytochrome in the ultracentrifugal field; the purity being estimated to be 50 to 70 per cent. A molecular weight of 600, 000 to 800, 000 could be expected for the cytochrome from its sedimentation constant. On the other hand, a
minimum molecular weight of about 160, 000 was obtained from the heme content of the cytochrome. The cytochrome could be split by acid acetone into protoheme and an apoprotein moiety. The recombination of the two components could be observed spectro-photometrically, but the reconstructed cytochrome was no more native as evidenced by its capabiliiy to combine with CO. The normal oxidation-reduction potential of purified cytochrome bt was determined to be about -20 mV at pH 7.0 and 25°C. Spectral properties, reactivity and chemical composition of the purified preparation were also studied.
We wish to thank Dr. A. Ohsaka of the Natio-nal Institute of Health, Tokyo, for a generous gift of snake venom, and Dr. K. Kakiuchi of the Institute for Protein Research, Osaka University, Osaka, for carrying out the ultracentrifugal analyses.},
 pages = {282--290},
 title = {Purification and Properties of Cytochrome b1 from Escherichia coli},
 volume = {53},
 year = {1963}
}