Results 301 to 310 of about 328,755 (334)
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Nonenzymic acetylation of histones with acetyl phosphate and acetyl adenylate
Biochemistry, 1975Nonenzymatic acetylation of calf-thymus lysine- and arginine-rich histones was demonstrated to occur when these proteins were incubated with [14C]acetyl phosphate and [14C]acetyl adenylate. The levels of acetylation depend on both pH and on reagent concentration.
RAMPONI, GIAMPIETRO+2 more
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Clonazepam acetylation in fast and slow acetylators
Clinical Pharmacology and Therapeutics, 1981Six slow acetylators (SAs) and six rapid acetylators (RAs), as determined by sulfamethazine (SMZ) phenotyping, were each given a 2-mg oral dose of clonazepam. Ninety-six-hour urine collections from these subjects were analyzed for clonazepam, 7-amino clonazepam (7-AM, clonazepam nitroreduced metabolite), and 7-acetamido clonazepam (7-ACT, N-acetylated ...
B. H. Min+11 more
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THE ACETYLATION OF PROTHROMBIN
Canadian Journal of Biochemistry and Physiology, 1960Purified bovine prothrombin was acetylated to a range of 27 to 30% of its amino groups. Except for just significant amounts it lost its power to generate thrombin-C. Upon activation the yield of thrombin-E was 100% on the basis of the thrombin-C yield that was obtained on an aliquot sample of the prothrombin before acetylation.
Ricardo H. Landaburu, Walter H. Seegers
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Acetyl-CoA, protein acetylation, and liver cancer
Molecular Cell, 2022Using multi-omics approaches, Park et al. show that reduced cellular acetyl-CoA and protein hypoacetylation promote liver cancer growth and dedifferentiation.
Zhengming, Wu, Kun-Liang, Guan
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Nonenzymatic acetylation of histones with acetyl-CoA
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970Abstract 1. When purified calf thymus histones were incubated with [1-14C]acetyl-CoA and treated to remove the acid-soluble fraction with trichloroacetic acid, a large amount of radioactivity still remained in the 15 % trichloroacetic acid-insoluble precipitate. 2.
Hyang Woo Lee+3 more
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Canadian Journal of Biochemistry and Physiology, 1959
Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p ...
Ricardo H. Landaburu, Walter H. Seegers
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Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p ...
Ricardo H. Landaburu, Walter H. Seegers
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Acetylation of Sulphanilamide by Acetyl Metaphosphate
Nature, 1950THE problem regarding the nature of the reactive, intermediate C2-compound in acetate metabolism is not clear at present. With regard to biological acetylations, it is evident, especially from Lipmann's1 work, that a strongly acetylating substance is formed in an enzymatic reaction between acetate and adenosine triphosphate.
Thomas Rosenberg, Hans E. Heyman
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Psychopharmacology, 1979
Microsome-free preparations of rodent and human liver were shown to contain N-acetyl transferase from experiments using procainamide as substrate. These preparations then acetylated phenelzine from the quantitative transfer of radiolabeled acetate. This in vitro demonstration of phenelzine acetylation in rodent and human liver was corroborated by the ...
Eve C. Johnstone+2 more
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Microsome-free preparations of rodent and human liver were shown to contain N-acetyl transferase from experiments using procainamide as substrate. These preparations then acetylated phenelzine from the quantitative transfer of radiolabeled acetate. This in vitro demonstration of phenelzine acetylation in rodent and human liver was corroborated by the ...
Eve C. Johnstone+2 more
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