A fast and efficient method for quantitative measurement of S-adenosyl-L-methionine-dependent methyltransferase activity with protein substrates

Analytical Biochemistry

Volumn 398, Issue 2, 2010, Pages 218-224

  Suh Lailam, Brenda B ^a   Hevel, Joan M ^a  

^a UTAH STATE UNIVERSITY   (United States)

Author keywords

AdoMet; Kinetic assay; Kinetics; Methyltransferase; PKMT; PRMT; Protein arginine methylation; Protein lysine methylation; Quantification of methyltransfer; S adenosyl methionine; SAM

Indexed keywords

ALKYLATION; ARGININE; ENZYME KINETICS; METHYLATION;

ADOMET; KINETIC ASSAY; METHYLTRANSFERASES; PKMT; PRMT; QUANTIFICATION OF METHYLTRANSFER; S-ADENOSYL METHIONINES;

PROTEINS;

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE; RESIN; S ADENOSYLMETHIONINE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; ISOTOPE LABELING; MICHAELIS MENTEN KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN METHYLATION; QUANTITATIVE ANALYSIS;

EID: 77649192714     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.09.005     Document Type: Article

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