Zobrazeno 1 - 10
of 98
pro vyhledávání: '"J. Rohlfs"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
J. Rohlfs
Publikováno v:
Mathematische Semesterberichte. 48:67-78
Die Aufgabe der Bestimmung aller moglichen Isometriegruppen von Objekten wie Ornamenten oder Kristallpackungen last sich bekanntlich als ein Problem der Gruppenkohomologie auffassen. Als eine Einfuhrung hierzu wird ein kohomologischer Ansatz zur Klas
Publikováno v:
Journal of Inorganic Biochemistry. 75:241-244
The ability of myoglobin (Mb) to reversibly bind O2 and other ligands has been well characterized. Mb also participates with a variety of redox metals to form metmyoglobin (metMb). By using an anaerobic stopped-flow device we have measured outer-sphe
Autor:
Shinji Takeoka, Amy G. Tsai, Ronald J. Rohlfs, Hiromi Sakai, Eishun Tsuchida, Marcos Intaglietta, Hiroyuki Hara
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 276:H553-H562
Phospholipid vesicles encapsulating purified hemoglobin (HbV) were developed to provide O2-carrying capacity to plasma expanders. Microvascular perfusion was determined for HbV with different O2affinity (P50= 9, 16, and 30 mmHg) prepared by coencapsu
Publikováno v:
Analytical Biochemistry. 256:107-116
A rapid, new method to measure hemoglobin-oxygen equilibrium curves is described using the protocatechuic acid/protocatechuic acid 3,4-dioxygenase system [C. Bull and D.P. Ballou (1981) J. Biol. Chem. 256, 12673-12680] to deoxygenate hemoglobin solut
Publikováno v:
Biophysical Chemistry. 69:23-30
Colloid osmotic pressures of hemoglobin solutions containing unmodified, intramolecularly cross-linked, intermolecularly polymerized, or polyethylene glycol (PEG) surface-conjugated hemoglobin have been measured to determine their macromolecular solu
Autor:
J. Rohlfs
Publikováno v:
Journal für die reine und angewandte Mathematik (Crelles Journal). 1996:149-182
Autor:
R J Rohlfs, R Hille
Publikováno v:
Journal of Biological Chemistry. 269:30869-30879
Publikováno v:
Journal of Biological Chemistry. 269:13942-13950
In trimethylamine dehydrogenase, the enzyme-bound FMN is covalently linked to Cys-30 by a 6-S-cysteinyl FMN bond. The role played by this bond in catalysis has been investigated using a recombinant wild-type trimethylamine dehydrogenase and a Cys-30
Publikováno v:
Mathematische Annalen. 296:191-214