Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Engin Halit Serpersu"'
Autor:
Engin Halit Serpersu, Holger Linnertz, Wilhelm Schoner, Evelyn Hamer, Zeljka Kovarik, Roberto Antolović, Holger Kost
Publikováno v:
European Journal of Biochemistry. 261:181-189
To test the hypothesis that Na+/K+-ATPase works as an (alpha beta)2-diprotomer with interacting catalytic alpha-subunits, tryptic digestion of pig kidney enzyme, that had been inactivated with substitution-inert MgATP complex analogues, was performed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53812f4fda782d0a69c320250da591fd
https://doi.org/10.1046/j.1432-1327.1999.00260.x
https://doi.org/10.1046/j.1432-1327.1999.00260.x
Autor:
Detlef Thönges, Evelyn Hamer, Engin Halit Serpersu, Roberto Antolović, M. Willeke, Wilhelm Schoner, Georgios Scheiner-Bobis, Engelbert Buxbaum
Publikováno v:
The Sodium Pump ISBN: 9783642725135
It is presently unclear whether the membrane-embedded sodium pump works as an (αs) monomer (4) according to the single site model (15,32) or as an (αs)2 diprotomer of interacting α subunits (21–23,33). The single site model includes as an essent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::084ed4948da1a91911023e5fa205a563
https://doi.org/10.1007/978-3-642-72511-1_53
https://doi.org/10.1007/978-3-642-72511-1_53
Publikováno v:
European journal of biochemistry. 191(2)
The exchange-inert tetra-ammino-chromium complex of ATP [Cr(NH3)4ATP], unlike the analogous cobalt complex Co(NH3)4ATP, inactivated Na+/K(+)-ATPase slowly by interacting with the high-affinity ATP binding site. The inactivation proceeded at 37 degree
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ec214712ea3c13849568b3aaa556abe
https://pubmed.ncbi.nlm.nih.gov/2166662
https://pubmed.ncbi.nlm.nih.gov/2166662
Publikováno v:
European journal of biochemistry. 157(3)
The chromium(III) complex of ATP, an MgATP complex analogue, inactivates (Na+ + K+)-ATPase by forming a stable chromo-phosphointermediate. The rate constant k2 of inactivation at 37 degrees C of the beta, gamma-bidentate of CrATP is enhanced by Na+ (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10a20cf35dd425b749821c2770b6f721
https://pubmed.ncbi.nlm.nih.gov/2424757
https://pubmed.ncbi.nlm.nih.gov/2424757