Lipid Specific Activation of the Murine P4-ATPase Atp8a1 (ATPase II)†

Biochemistry ◽  
2006 ◽  
Vol 45 (16) ◽  
pp. 5367-5376 ◽  
Author(s):  
Jill K. Paterson ◽  
Kathleen Renkema ◽  
Lisa Burden ◽  
Margaret S. Halleck ◽  
Robert A. Schlegel ◽  
...  
Keyword(s):  
Atpase Ii

Appearance of voltage-gated calcium channels following overexpression of ATPase II cDNA in neuronal HN2 cells

2003 ◽  
Vol 117 (2) ◽  
pp. 109-115 ◽  
Author(s):  
Gary Chin ◽  
Yasir El-Sherif ◽  
Farah Jayman ◽  
Rima Estephan ◽  
Andrzej Wieraszko ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
Atpase Ii

scholarly journals Identification and Functional Expression of Four Isoforms of ATPase II, the Putative Aminophospholipid Translocase

2000 ◽  
Vol 275 (30) ◽  
pp. 23378-23386 ◽  
Author(s):  
Jiantao Ding ◽  
Zhao Wu ◽  
Bill P. Crider ◽  
Yongming Ma ◽  
Xinji Li ◽  
...  
Keyword(s):  
Functional Expression ◽  
Aminophospholipid Translocase ◽  
Atpase Ii

Is there a plasma-membrane-located anion-sensitive ATPase? II. Further studies on rabbit kidney

1977 ◽  
Vol 471 (1) ◽  
pp. 78-91 ◽  
Author(s):  
J.M.M. van Amelsvoort ◽  
J.J.H.H.M. de Pont ◽  
A.L.H. Stols ◽  
S.L. Bonting
Keyword(s):  
Plasma Membrane ◽  
Rabbit Kidney ◽  
Atpase Ii

scholarly journals Isolation of ATPase I, the proton pump of chromaffin-granule membranes

1985 ◽  
Vol 231 (3) ◽  
pp. 557-564 ◽  
Author(s):  
J M Percy ◽  
J G Pryde ◽  
D K Apps
Keyword(s):  
Proton Pump ◽  
Alkylating Agents ◽  
Proton Translocation ◽  
Phase Segregation ◽  
Chromaffin Granule ◽  
Chromaffin Granule Ghosts ◽  
Triton X ◽  
Atpase Ii ◽  
Hydrolysis Of ◽  
Granule Matrix

Chromaffin-granule membranes contain two ATPases, which can be separated by (NH4)2SO4 fractionation after solubilization with detergents, or by phase segregation in Triton X-114. ATPase I (Mr 400000) is inhibited by trialkyltin, quercetin and alkylating agents, and hydrolyses both ATP and ITP. It contains up to five types of subunit, including a low-Mr hydrophobic polypeptide that reacts with dicyclohexylcarbodi-imide; these subunits are unrelated to those of mitochondrial F1F0-ATPase, as judged by size and reaction with antibodies. ATPase II (Mr 140000) is inhibited by vanadate, and is specific for ATP; it has not been extensively purified. Proton translocation by resealed chromaffin-granule ‘ghosts’, measured by uptake of methylamine or by quenching of the fluorescence of 9-amino-6-chloro-2-methoxyacridine, is supported by the hydrolysis of ATP or ITP, and inhibited by quercetin or alkylating agents, but not by vanadate. ATPase I must therefore be the proton translocator involved in the uptake of catecholamines and possibly of other components of the chromaffin-granule matrix, whereas ATPase II does not translocate protons.

Genotypes of sarco(endo)plasmic reticulum Ca2+-dependent ATPase II gene in substrains of spontaneously hypertensive rats

1996 ◽  
Vol 14 (3) ◽  
pp. 287-281 ◽  
Author(s):  
Yoichi Ohno ◽  
Koichi Matsuo ◽  
Hiromichi Suzuki ◽  
Hisao Tanase ◽  
Hiroko Ikeshima ◽  
...  
Keyword(s):  
Spontaneously Hypertensive Rats ◽  
Hypertensive Rats ◽  
Spontaneously Hypertensive ◽  
Dependent Atpase ◽  
Plasmic Reticulum ◽  
Atpase Ii

scholarly journals 3P151 Giant Acceleration of diffusion in F1-ATPase II(Molecular motor,Poster,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))

2014 ◽  
Vol 54 (supplement1-2) ◽  
pp. S274
Author(s):  
Hayashi Ryunosuke ◽  
Nakamura Shuichi ◽  
Kudo Seishi ◽  
Sasaki Kazuo ◽  
Noji Hiroyuki ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Molecular Motor ◽  
F1 Atpase ◽  
Biophysical Society ◽  
Atpase Ii
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