Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Marianne Frolich"'
Autor:
Marianne Frolich
Publikováno v:
Journal of Cellular Physiology. 109:439-445
We have partially purified a mitogenic factor, termed colony stimulating factor, which is secreted from a human T lymphocytic cell line, and which stimulates in vitro formation of colonies of macrophages and granulocytes by human bone marrow cells. C
Publikováno v:
Archives of Biochemistry and Biophysics. 189:471-480
Detailed stopped-flow kinetic studies of the association of 2,2-bipyridine, 1,10-phenanthroline, and 5-chloro-1,10-phenanthroline to the zinc ion at the active site of alcohol dehydrogenase have demonstrated that a process with a limiting rate consta
Publikováno v:
Journal of Biological Chemistry. 257:10582-10586
Particulate adenylate cyclase preparations from rat uterine smooth muscle had a single class of [3H]guanyl-5'-yl imidodiphosphate ([3H]GMP.P(NH)P)-binding sites with all of the properties of the guanyl nucleotide-requiring enzyme activation sites (N)
Publikováno v:
Journal of Biological Chemistry. 256:5436-5442
Publikováno v:
Archives of Biochemistry and Biophysics. 217:473-478
The activation of uterine smooth muscle adenylate cyclase was studied by pretreating the particulate form of the enzyme with the GTP analog guanyl-5′-yl imidodiphosphate (Gpp(NH)p). Pretreatment with Gpp(NH)p left the enzyme in an irreversibly acti
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 286:155-163
1. 1. Rat liver glucose-6-phosphate dehydrogenase has been used to test the hypotheses that unsaturated fatty acids inhibit this enzyme in vivo or act as co-pressors regulating the synthesis of lipogenic enzymes. When rats are switched from a non-fat
Publikováno v:
Archives of biochemistry and biophysics. 226(1)
Adenylate cyclase was extracted from the rat uterus with Lubrol PX in a form which remained soluble following centrifugation for 60 min at 100,000 g . The soluble enzyme was stimulated by both Mn 2+ and by guanyl-5′-yl-imidodiphosphate (Gpp(NH)p),
Publikováno v:
European journal of biochemistry. 126(3)
The oximes of aliphatic aldehydes inhibit horse liver and yeast alcohol dehydrogenase. The pattern of inhibition of these enzymes by the oximes reflects their substrate specificity. For example, acetaldoxime is a more effective inhibitor of the yeast