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M A Rimpil?inen T T Mett?nen K Niskasaari R I Forsén 《The International journal of biochemistry》1988,20(10):1117-1124
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. 相似文献
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Kaarina Niskasaari Katri M.S. Juutinen Marja A. Rimpiläinen Raili Forsén† 《Letters in applied microbiology》1988,6(6):157-160
The presence of lipoteichoic acid (LTA) in plasma membrane and released adenosine triphosphatase (ATPase) preparations of Streptococcus lactis subsp. cremoris HA was studied by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The membrane preparation gave two spots with periodic acid Schiff's (PAS) staining. The reference LTA revealed one CBB stainable band with MW 21 500, and was detected as a characteristic yellow spot in the molecular weight area 14 000–20 900 with silver staining and was also stainable with PAS. A slight colour was found with PAS in the F1 -ATPase (EC 3.6.1.3) preparation. The results suggest that the carbohydrate component in the membrane preparation and in the solubilized F1 -ATPase is LTA. 相似文献
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