Quantitative identification of N-terminal amino acids in proteins by radiolabeled reductive methylation and amino acid analysis: Application to human erythrocyte acetylcholinesterase
- 1 July 1985
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 148 (1) , 154-162
- https://doi.org/10.1016/0003-2697(85)90640-2
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Identification of lysine residues essential for microtubule assembly. Demonstration of enhanced reactivity during reductive methylation.Journal of Biological Chemistry, 1983
- Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region.Journal of Biological Chemistry, 1982
- Reductive methylation of proteins with sodium cyanoborohydride. Identification, suppression and possible uses of N-cyanomethyl by-productsBiochemical Journal, 1982
- Simple, rapid, and highly efficient separation of amino acid phenylthiohydantoins by reversed-phase high-performance liquid chromatographyAnalytical Biochemistry, 1982
- Characterization of pepsin-resistant collagen-like tail subunit fragments of 18S and 14S acetylcholinesterase from Electrophorus electricusBiochemistry, 1981
- Labeling of proteins by reductive methylation using sodium cyanoborohydride.Journal of Biological Chemistry, 1979
- Studies on the characterization of human erythrocyte acetylcholinesterase and its interaction with antibodiesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- The primary structure of bovine prolactinFEBS Letters, 1974
- The Disulfide Bonds of Egg White Lysozyme (Muramidase)Journal of Biological Chemistry, 1965
- A new and rapid colorimetric determination of acetylcholinesterase activityBiochemical Pharmacology, 1961