PMID: 2907882Jan 1, 1988

The F1-ATPase from Streptococcus cremoris: isolation, purification and partial characterization

The International Journal of Biochemistry
M A RimpiläinenR I Forsén


1. The F1-ATPase from the plasma membrane of Streptococcus cremoris HA was released by low ionic shock wash and purified by gel filtration and ion exchange chromatography. 2. The specific activity of the purified F1-ATPase was 25.8 mumol Pi/mg protein/min. 3. Km for ATP was 0.80 mM, and Ki for ADP as a competetive inhibitor 0.40 mM. 4. The purified F1-ATPase consisted of five subunits, alpha, beta, gamma, delta and epsilon, with molecular masses of 47.0, 45.0, 29.5, 22.0 and 13.0 kDa, respectively. 5. The isoelectric point of the enzyme complex was found to be 4.4.


Sep 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·P Owen, M R Salton
Apr 5, 1976·Biochemical and Biophysical Research Communications·A AbramsD H Morris
Apr 1, 1976·Journal of General Microbiology·T W Ritchey, H W Seely
Jun 1, 1987·Journal of Dental Research·S V Sutton, R E Marquis
Jan 1, 1987·The International Journal of Biochemistry·M A Rimpiläinen
Oct 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·P C MaloneyT H Wilson
Oct 12, 1971·Biochimica Et Biophysica Acta·R W Bonsall, S Hunt
Dec 1, 1982·European Journal of Biochemistry·S F BiketovV L Tsuprun
Sep 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·R OttoW N Konings
Sep 1, 1983·Antonie van Leeuwenhoek·W N Konings, R Otto
Dec 21, 1981·Biochimica Et Biophysica Acta·B M Kubak, W W Yotis

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