1990
DOI: 10.1016/0005-2728(90)90171-y
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The F1-type ATPase in anaerobic Lactobacillus casei

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Cited by 7 publications
(2 citation statements)
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“…In contrast, the levels of inhibition of MB F 1Ec (or F 1 F oEc ) at the above concentrations of DCCD and Na azide were between 92 and 98%. A higher tolerance of MB and soluble F 1 F oCp or F 1Cp to inhibition by DCCD and Na azide is not unusual, as similar results were reported for several gram-positive bacteria (3,26,28,32,49). A comparison of the ATPase activities of DM-and EDTA-extracted membranes with that of untreated membranes indicated that about 87 and 70% of ATPase activities were solubilized from membranes by DM and EDTA, respectively ( Table 2).…”
Section: I) Atpb(a) Atpe(c) Atpf(b) Atph(␦) Atpa(␣) Atpg(␥) Atsupporting
confidence: 80%
“…In contrast, the levels of inhibition of MB F 1Ec (or F 1 F oEc ) at the above concentrations of DCCD and Na azide were between 92 and 98%. A higher tolerance of MB and soluble F 1 F oCp or F 1Cp to inhibition by DCCD and Na azide is not unusual, as similar results were reported for several gram-positive bacteria (3,26,28,32,49). A comparison of the ATPase activities of DM-and EDTA-extracted membranes with that of untreated membranes indicated that about 87 and 70% of ATPase activities were solubilized from membranes by DM and EDTA, respectively ( Table 2).…”
Section: I) Atpb(a) Atpe(c) Atpf(b) Atph(␦) Atpa(␣) Atpg(␥) Atsupporting
confidence: 80%
“…A number of attempts have been made to determine relative molar subunit stoichiometries of multi-subunit protein complexes from scanned electrophoresis profiles after protein staining with Coomassie Brilliant Blue dye [20][21][22][23][24][25][26][27][28][29]. The quantitative reliability of such measurements is questionable, however, especially considering that staining intensity for this dye is only quantitatively related to protein mass when comparing identical or very similar proteins.…”
Section: Discussionmentioning
confidence: 99%