Zobrazeno 1 - 10
of 10
pro vyhledávání: '"H M, Scofano"'
Publikováno v:
The Journal of biological chemistry. 271(31)
Erythrosin B was used to photo-oxidize the sarcoplasmic reticulum Ca2+-ATPase. The ATPase activity is rapidly and irreversibly inhibited by photo-oxidation with erythrosin. This inhibition is protected by the presence of ATP during the photo-oxidatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d10c10d91c57fada3b9a9cb45353bd27
https://pubmed.ncbi.nlm.nih.gov/8702486
https://pubmed.ncbi.nlm.nih.gov/8702486
Publikováno v:
The Journal of biological chemistry. 268(35)
Troponin C can replace calmodulin in the activation of the Ca(2+)-ATPase of pig erythrocytes provided that the reaction medium contains relatively high free Ca2+ concentrations (0.5 microM). In the presence of 10 microM free Ca2+, the troponin C-acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e8814f449052aba9b25826ee1cd0102
https://pubmed.ncbi.nlm.nih.gov/8253742
https://pubmed.ncbi.nlm.nih.gov/8253742
Publikováno v:
Biochimica et biophysica acta. 1039(3)
The analog of ATP obtained by oxidation of the ribose ring of ATP with periodate (oxATP) was used as a reagent for the inhibition and labeling of the Ca2(+)-ATPase purified from sarcoplasmic reticulum membranes. The substrate concentration dependence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4e53e1906627925602b7d1bcb21a0c9f
https://pubmed.ncbi.nlm.nih.gov/2143085
https://pubmed.ncbi.nlm.nih.gov/2143085
Autor:
P C Carvalho-Alves, H M Scofano
Publikováno v:
Journal of Biological Chemistry. 262:6610-6614
The hydrolytic cycle of sarcoplasmic reticulum Ca2+-ATPase in the absence of Ca2+ was studied. At pH 6.0, 10 degrees C and in the absence of K+, the enzyme displays a very low velocity of ATP hydrolysis. Addition of up to 15% dimethyl sulfoxide incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::854000c45ed5013c00040169ff47e5fe
https://doi.org/10.1016/s0021-9258(18)48285-3
https://doi.org/10.1016/s0021-9258(18)48285-3
Autor:
H M Scofano, P C Carvalho-Alves
Publikováno v:
Journal of Biological Chemistry. 258:3134-3139
(Ca2+ + Mg2+)-dependent ATPase purified from sarcoplasmic reticulum was phosphorylated by [gamma-32P]ATP in the presence of ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, dimethyl sulfoxide, and magnesium up to levels of 1.0 m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33393f85cf79ccc7ab97935b00428247
https://doi.org/10.1016/s0021-9258(18)32841-2
https://doi.org/10.1016/s0021-9258(18)32841-2
Autor:
P C, Carvalho-Alves, H M, Scofano
Publikováno v:
The Journal of biological chemistry. 262(14)
The hydrolytic cycle of sarcoplasmic reticulum Ca2+-ATPase in the absence of Ca2+ was studied. At pH 6.0, 10 degrees C and in the absence of K+, the enzyme displays a very low velocity of ATP hydrolysis. Addition of up to 15% dimethyl sulfoxide incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5783b3cbfd6be0ed3805c8dc548afe29
https://pubmed.ncbi.nlm.nih.gov/2952654
https://pubmed.ncbi.nlm.nih.gov/2952654
Publikováno v:
Biochemistry. 24(4)
Treatment of sarcoplasmic reticulum adenosinetriphosphatase (ATPase) with N,N'-dicyclohexylcarbodiimide is known to produce total inhibition of calcium binding and enzyme activity. However, we now find that treatment with lower reagent:protein ratios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9ab6af247f767df195b78c7b08a64532
https://pubmed.ncbi.nlm.nih.gov/3158344
https://pubmed.ncbi.nlm.nih.gov/3158344
Autor:
P C, Carvalho-Alves, H M, Scofano
Publikováno v:
The Journal of biological chemistry. 258(5)
(Ca2+ + Mg2+)-dependent ATPase purified from sarcoplasmic reticulum was phosphorylated by [gamma-32P]ATP in the presence of ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, dimethyl sulfoxide, and magnesium up to levels of 1.0 m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8b9824d9b9a3aba6eb6987996627b3b3
https://pubmed.ncbi.nlm.nih.gov/6219109
https://pubmed.ncbi.nlm.nih.gov/6219109
Autor:
H M, Scofano, L, de Meis
Publikováno v:
The Journal of biological chemistry. 256(9)
The reversibility of the reaction catalyzed by purified (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum was studied by measuring the rates of synthesis and hydrolysis of ATP observed during the ATP in equilibrium Pi exchange reaction. The ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e24dc24e1c2d4418ff5aa66c412a9b9f
https://pubmed.ncbi.nlm.nih.gov/6111563
https://pubmed.ncbi.nlm.nih.gov/6111563
Publikováno v:
The Journal of biological chemistry. 254(20)
The rate of phosphorylation of the Ca2+-dependent ATPase of sarcoplasmic reticulum vesicles by ITP and ATP was studied using a millisecond mixing and quenching device. The rate of phosphorylation was slower when the vesicles were preincubated in a Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::191ec70172bd5e9a94e9b79f6b077091
https://pubmed.ncbi.nlm.nih.gov/158593
https://pubmed.ncbi.nlm.nih.gov/158593