Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Arthur Kowalsky"'
Autor:
Jay L. Bock, Arthur Kowalsky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 526:135-146
31P nuclear magnetic resonance spectra and enzymatic activities are compared for alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) species with different zinc contents. The enzyme containing two Zn2+ per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9d731a4dd619f83f51365402b06cd6c
https://doi.org/10.1016/0005-2744(78)90298-x
https://doi.org/10.1016/0005-2744(78)90298-x
Autor:
D. J. Boone, Arthur Kowalsky
Publikováno v:
Biochemistry. 13:731-738
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b19ab3d66201f5be8ba72aa5f52c679
https://doi.org/10.1021/bi00701a015
https://doi.org/10.1021/bi00701a015
Publikováno v:
Journal of Biological Chemistry. 244:502-505
Alkali ion complex formation by the cyclic depsipeptide, valinomycin, has been studied by means of nuclear magnetic resonance spectroscopy. Characteristic perturbations of the positions and fine structures of the resonances of the protons of specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c16660fdfc967c3636590497ef14c803
https://doi.org/10.1016/s0021-9258(18)94458-3
https://doi.org/10.1016/s0021-9258(18)94458-3
Publikováno v:
Journal of Biological Chemistry. 234:2627-2634
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d97167efcc09db8970014d9928aa1d3
https://doi.org/10.1016/s0021-9258(18)69749-2
https://doi.org/10.1016/s0021-9258(18)69749-2
Publikováno v:
Journal of Biological Chemistry. 219:719-725
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18c89a6e77d12a73f75b9b1cd6319706
https://doi.org/10.1016/s0021-9258(18)65731-x
https://doi.org/10.1016/s0021-9258(18)65731-x
Publikováno v:
Journal of Biological Chemistry. 211:279-287
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c90d2f1ffdee5b54cde3da12688da5be
https://doi.org/10.1016/s0021-9258(18)71218-0
https://doi.org/10.1016/s0021-9258(18)71218-0
Autor:
P.D. Boyer, Arthur Kowalsky
Publikováno v:
Journal of Biological Chemistry. 235:604-608
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e23e7d3582ab34d2f322edd583413ee
https://doi.org/10.1016/s0021-9258(19)67912-3
https://doi.org/10.1016/s0021-9258(19)67912-3
Autor:
Arthur Kowalsky
Publikováno v:
Biochemistry. 4:2382-2388
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3d72426f9269e6fffca487c4ad98aae
https://doi.org/10.1021/bi00887a018
https://doi.org/10.1021/bi00887a018
Autor:
Sarah Ratner, Arthur Kowalsky
Publikováno v:
Biochemistry. 8:899-907
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bad752fe640325f2ca063356b4ca0549
https://doi.org/10.1021/bi00831a020
https://doi.org/10.1021/bi00831a020
Autor:
Arthur Kowalsky
Publikováno v:
Journal of Biological Chemistry. 244:6619-6625
Cytochrome c is swiftly and quantitatively reduced by chromous ion. In the course of the reduction chromium is bound to the protein. At pH 4.78 and 7.0 the ratio of chromium to cytochrome c is approximately 0.5 mole per mole. When phosphate is presen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::077140e10d53e3467ad97786e1614e2c
https://doi.org/10.1016/s0021-9258(18)63451-9
https://doi.org/10.1016/s0021-9258(18)63451-9