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Protocols
Enzymatic Assay and ATP Sensitivity Test of Luciferase
1. OBJECTIVE To standardize a procedure to determine the enzymatic activity of Luciferase and/or to determine the ATP detection limit of Luciferase.
Keywords: Biochemistry, Enzyme activity, Enzymology, Size-exclusion chromatography
Enzymatic Assay of Achromopeptidase
1. OBJECTIVE The objective of this procedure is to standardize a method for the enzymatic assay of Achromopeptidase.
Keywords: Clinical, Microbiology
Enzymatic Assay of Carbonic Anhydrase for Wilbur-Anderson Units (EC 4.2.1.1)
1. OBJECTIVE To standardize a procedure for the enzymatic assay of Carbonic Anhydrase (EC 4.2.1.1) for Wilbur-Anderson Units.
Keywords: Hydration reaction, Phase transitions
Enzymatic Assay of Carboxypeptidase A
1. OBJECTIVE To standardize a procedure for the assay of Carboxypeptidase A at Sigma-Aldrich, St. Louis.
Keywords: Extinction coefficient
Enzymatic Assay of Chloramphenicol Acetyltransferase
1. OBJECTIVE To standardize a procedure for the determination of the enzymatic assay of Chloramphenicol Acetyltransferase.
Keywords: Enzyme activity, Enzymology, Extinction coefficient
Enzymatic Assay of Chymotrypsin (EC 3.4.21.1)
2. SCOPE The scope of this procedure includes products that have a specification for Chymotrypsin activity. This assay procedure is not to be used to assay Chymotrypsin, Insoluble, Sigma-Aldrich Prod...
Keywords: Extinction coefficient
Enzymatic Assay of Elastase
2. SCOPE This assay procedure applies to all products that have specification for the enzymatic activity of Elastase using SucALA3 as a substrate at Sigma-Aldrich Saint Louis.
Keywords: Enzyme activity, Extinction coefficient
Enzymatic Assay of Protease, Product No. P2922
1. OBJECTIVE To standardize a procedure for the enzymatic assay of Protease activity with N-t-Boc-L-glutamic acid α-phenyl ester substrate.
Keywords: Digestions, Enzymology, Extinction coefficient
Enzymatic Assay of Trypsinogen
1. OBJECTIVE To standardize a procedure for the determination of the enzymatic assay of trypsinogen.
Keywords: Enzyme activity, Extinction coefficient
Papers
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Zinc binding ligands and cellular zinc trafficking: apo-metallothionein, glutathione, TPEN, proteomic zinc, and Zn-Sp1. Ujala Rana et al J. Inorg. Biochem. 102, 489-99, (2008)
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Quantifying the energetic contributions of desolvation and π-electron density during translesion DNA synthesis. Edward A. Motea et al Nucleic Acids Res. 39, 1623-37, (2011)
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Developing structure-activity relationships for the prediction of hepatotoxicity. Nigel Greene et al Chem. Res. Toxicol. 23, 1215-22, (2010)
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A predictive ligand-based Bayesian model for human drug-induced liver injury. Sean Ekins et al Drug Metab. Dispos. 38, 2302-8, (2010)
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Translating Clinical Findings into Knowledge in Drug Safety Evaluation - Drug Induced Liver Injury Prediction System (DILIps). Zhichao Liu et al PLoS Comput. Biol. 7, e1002310, (2011)
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Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Molloy, M.P., et al. Electrophoresis 19, 837, (1998)
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Membrane proteins and proteomics: un amour impossible? Santoni, V., et al. Electrophoresis 21, 1054, (2000)
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Merck 14,9772
Beil. 4,IV,1903
Aldrich MSDS 1, 1815:C / Corp MSDS 1 (2), 3532:A / FT-IR 1 (1), 347:C / FT-IR 2 (1), 542:D / IR-Spectra (3), 203:G / IR-Spectra (2), 183:E / IR-Spectra (2), 183:D / IR-Spectra (3), 203:H / NMR-Reference 2 (1), 304:A / RegBook 1 (1), 371:C / Sax 6, 2558 / Sigma FT-IR 1 (2), 60:D / Sigma FT-IR 1 (2), 61:C / Structure Index 1, 52:C:5 / Vapor Phase 3, 437:C