bafilomycin-a1 and sodium-nitrate

bafilomycin-a1 has been researched along with sodium-nitrate* in 2 studies

Other Studies

2 other study(ies) available for bafilomycin-a1 and sodium-nitrate

Article	Year
Is the Paracoccus halodenitrificans ATPase a chimeric enzyme? FEMS microbiology letters, 1996, Jun-15, Volume: 140, Issue:1 Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases. Topics: Adenosine Triphosphatases; Anti-Bacterial Agents; Azides; Dicyclohexylcarbodiimide; Enzyme Inhibitors; Ethylmaleimide; Macrolides; Membranes; Nitrates; Paracoccus; Potassium Chloride; Proton-Translocating ATPases; Rhodamines; Sodium Chloride; Vacuolar Proton-Translocating ATPases	1996
A pharmacological assessment of the mammalian osteoclast vacuolar H(+)-ATPase. Bone and mineral, 1994, Volume: 27, Issue:2 It is well established that osteoclasts use a vacuolar-type H(+)-ATPase (V-ATPase) for proton pumping during bone resorption and that specific V-ATPase inhibitors such as bafilomycin A1 abolish osteoclastic bone resorption in the bone slice assay. It has been reported that the V-ATPase in avian osteoclasts can be distinguished from the V-ATPase expressed in most other cells, by virtue of its inhibition by vanadate and nitrate ions. In order to determine whether the V-ATPase in mammalian osteoclasts can be similarly distinguished, we have investigated the effects of vanadate and nitrate on bone resorption by rat osteoclasts in the bone slice assay, in comparison with known V-ATPase inhibitors, bafilomycin A1 and WY 47766, that also inhibit the chicken osteoclast V-ATPase. The results indicate that, unlike the avian osteoclast V-ATPase, the mammalian osteoclast V-ATPase is pharmacologically similar to the V-ATPase in other cells. Topics: Animals; Anti-Bacterial Agents; Bone Resorption; Cells, Cultured; Dose-Response Relationship, Drug; Femur; Imidazoles; Macrolides; Nitrates; Osteoclasts; Proton Pumps; Proton-Translocating ATPases; Pyridines; Rats; Sodium Chloride; Tibia; Vanadates	1994

Article

Year

Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?

FEMS microbiology letters, 1996, Jun-15, Volume: 140, Issue:1

Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.

Topics: Adenosine Triphosphatases; Anti-Bacterial Agents; Azides; Dicyclohexylcarbodiimide; Enzyme Inhibitors; Ethylmaleimide; Macrolides; Membranes; Nitrates; Paracoccus; Potassium Chloride; Proton-Translocating ATPases; Rhodamines; Sodium Chloride; Vacuolar Proton-Translocating ATPases

1996

A pharmacological assessment of the mammalian osteoclast vacuolar H(+)-ATPase.

Bone and mineral, 1994, Volume: 27, Issue:2

It is well established that osteoclasts use a vacuolar-type H(+)-ATPase (V-ATPase) for proton pumping during bone resorption and that specific V-ATPase inhibitors such as bafilomycin A1 abolish osteoclastic bone resorption in the bone slice assay. It has been reported that the V-ATPase in avian osteoclasts can be distinguished from the V-ATPase expressed in most other cells, by virtue of its inhibition by vanadate and nitrate ions. In order to determine whether the V-ATPase in mammalian osteoclasts can be similarly distinguished, we have investigated the effects of vanadate and nitrate on bone resorption by rat osteoclasts in the bone slice assay, in comparison with known V-ATPase inhibitors, bafilomycin A1 and WY 47766, that also inhibit the chicken osteoclast V-ATPase. The results indicate that, unlike the avian osteoclast V-ATPase, the mammalian osteoclast V-ATPase is pharmacologically similar to the V-ATPase in other cells.

Topics: Animals; Anti-Bacterial Agents; Bone Resorption; Cells, Cultured; Dose-Response Relationship, Drug; Femur; Imidazoles; Macrolides; Nitrates; Osteoclasts; Proton Pumps; Proton-Translocating ATPases; Pyridines; Rats; Sodium Chloride; Tibia; Vanadates

1994