Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Harold J. Strecker"'
Publikováno v:
Biochemical and biophysical research communications. 15(2)
This laboratory has reported previously that fragmentation of brain mitochondrial fractions resulted in a 7–25 fold increase of the antimycin A-sensitive NADH oxidase, provided that ionic compounds such as inorganic phosphate were present in the in
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 429:780-797
Ornithine-oxo-acid aminotransferase (EC 2.6.1.13) from rat kidney was prepared as a single homogeneous protein as judged by polyacrylamide gel electrophoresis, ultracentrifuge analysis and double diffusion precipitin test. Content of pyridoxal phosph
Autor:
Harold J. Strecker, T F Shen
Publikováno v:
Biochemical Journal. 150:453-461
Human lung fibroblasts (WI-38) in late exponential phase of growth, in stationary phase after confluency was reached, and at high or low number of population doublings were used to investigate the synthesis of proline and hydroxyproline from glutamat
Autor:
Harold J. Strecker, Isaac Harary
Publikováno v:
Journal of Biological Chemistry. 211:263-270
Autor:
Harold J. Strecker, Seymour Korkes
Publikováno v:
Journal of Biological Chemistry. 196:769-784
Publikováno v:
Endocrinology. 72:764-770
Recent studies of the 3β-hydroxysteroid dehydrogenase of rat liver have revealed that the magnitude of the sex difference previously reported (1, 2) depends on the concentration of tissue used for the assay. With low tissue concentrations, enzymatic
Autor:
Harold J. Strecker, Eva Eliasson
Publikováno v:
Journal of Biological Chemistry. 241:5750-5756
During the normal 4-day growth cycle of Chang's liver cells in tissue culture, ornithine δ-transaminase increased and returned to the initial level in a fairly regular and reproducible manner. These changes in activity appeared to be the net result
Autor:
Harold J. Strecker, George A. Kaysen
Publikováno v:
Biochemical Journal. 133:779-788
l-Arginase from rat kidney was partially purified and some properties were compared with those of l-arginase of rat liver. The kidney enzyme was firmly bound to the mitochondrial fraction and after solubilization required arginine or an unknown facto
Autor:
Harold J. Strecker, Jack Peisach
Publikováno v:
Journal of Biological Chemistry. 237:2255-2260
Autor:
Harold J. Strecker, Severo Ochoa
Publikováno v:
Journal of Biological Chemistry. 209:313-326