Results 361 to 370 of about 218,218 (394)
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CBP, a transcriptional coactivator and acetyltransferase

Biochemistry and Cell Biology, 2001
The CREB binding protein (CBP) was first identified as a protein that specifically binds to the active phosphorylated form of the cyclic-AMP response element binding protein (CREB). CBP was initially defined as a transcriptional coactivator that, as a result of its large size and multiple protein binding domain modules, may function as a molecular ...
Michael J. Hendzel, Kirk J. McManus
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Chloramphenicol Acetyltransferase Assay

Cold Spring Harbor Protocols, 2010
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
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Regulation of Arylamine N-Acetyltransferases

Current Drug Metabolism, 2008
Acetylation catalysed by the arylamine N-acetyltransferases (NATs; 2.3.1.5) is a major biotransformation pathway for arylamine and hydrazine drugs, as well as many carcinogens that we are exposed to on a daily basis. These compounds can either be detoxified by NATs or bioactivated to metabolites that have the potential to cause toxicity such as cancer.
Butcher, Neville J.   +2 more
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Automation of a chloramphenicol acetyltransferase assay

Analytical Biochemistry, 1990
Accurate quantification of chloramphenicol acetyltransferase (CAT) enzyme activity in a large number of samples has been achieved through robotization of a CAT assay on a laboratory workstation (Biomek 1000). The basic principle of this CAT assay relies on the selective diffusion of [3H]acetylchloramphenicol into a water-immiscible liquid scintillation
Daniel Astinotti   +2 more
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Fluorescent reporters of the histone acetyltransferase

Analytical Biochemistry, 2008
Histone acetyltransferases (HATs) are important chromatin modifying enzymes that catalyze acetylation of specific lysine residues in histone and nonhistone substrates. They participate in multiple cellular processes such as transcriptional regulation and signal transduction.
Yujun George Zheng, Jiang Wu
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Spectrophotometric assay for choline acetyltransferase

Analytical Biochemistry, 1972
Abstract A rapid and simple spectrophotometric assay for choline acetyltransferase is described. The method employs 4,4′-dithiodipyridine to measure the coenzyme A produced by the enzymic reaction. The conditions of the assay are described. The results are compared with those obtained by the radiochemical assay of the enzyme.
Li-Pen Chao, Frederick Wolfgram
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Choline acetyltransferase in corneal epithelium

Experimental Eye Research, 1973
Abstract The activity of choline acetyltransferase (EC 2.3.1.6.), the enzyme involved in the synthesis of acetylcholine, was measured by radiochemical assay in homogenates of epithelial cells scraped or cultured from rabbit cornea. The method involves the use of 1- 14 C acetyl-CoA and choline as substrates, resulting in the production of 1- 14 C ...
M.C. Gnädinger   +2 more
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Chloramphenicol Acetyltransferases

Annual Review of Biophysics and Biophysical Chemistry, 1989
W V, Shaw, A G, Leslie
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Chloroplastic Carnitine Acetyltransferase

1997
Carnitine acetyltransferase ( CAT ) is known to exist in plant mitochondria (spe review [ 2 ]). CAT catalyses the reversible reaction Carnitine + short-chain acyl CoA short-chain acylcarnitine + CoASH and is involved in the transport of activated acetyl moieties from the mitochondrion.
C. Masterson   +2 more
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