Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference12 articles.
1. Inactivation of Class I Fructose Diphosphate Aldolases by the Substrate Analog N-Bromoacetylethanolamine Phosphate
2. An Exploration of the Active Site of Aldolase Using Structural Analogs of Fructose Diphosphate*
3. [34a] Carboxymethylation
4. Analysis of carboxymethylated residues in proteins by an isotopic method, and its application to the bromoacetate-ribonuclease reaction
5. Haloacetol phosphates. Identification of the sulfhydryl group of rabbit muscle aldolase alkylated by chloroacetol phosphate. VI
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1. N-Bromoacetylethanolamine Phosphate as a Probe for the Identification of a Liver Microsomal Glucose-6-Phosphate Transporter Peptide in Rats and Ehrlich Ascites Tumor-Bearing Mice;Archives of Biochemistry and Biophysics;2000-05
2. Structure of a Fructose-1,6-bis(phosphate) Aldolase Liganded to Its Natural Substrate in a Cleavage-Defective Mutant at 2.3 Å,;Biochemistry;1999-09-01
3. Inhibition of the glucose-6-phosphatase system by N-bromoacetylethanolamine phosphate, a potential affinity label for auxiliary proteins;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-10
4. A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation;"Protein Engineering, Design and Selection";1996
5. Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects;Progress in Biophysics and Molecular Biology;1995
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