Arrangement of hydrophobic portions on the active surface of cholinesterase

Autor:	N. N. Godovikov, S. S. Mikhailov, V. I. Rozengart, M. I. Kabachnik, R. V. Sitkevich, A. A. Abdubakhabov
Rok vydání:	1968
Předmět:	Crystallography Reaction rate constant biology Stereochemistry Chemistry Alkoxy group biology.protein General Chemistry Active surface Esterase Cholinesterase
Zdroj:	Bulletin of the Academy of Sciences of the USSR Division of Chemical Science. 17:719-723
ISSN:	1573-9171 0568-5230
DOI:	10.1007/bf00905739
Popis:	1. The rate constants of the interaction of O-n-alkyl-S-(β-ethylmercaptoethyl) methylthiophosphonates and their methylsulfomethylates with cholinesterase were determined. 2. The anticholinesterase activity of the investigated compound depends greatly upon the length of the alkoxyl group. 3. Evidently there are several hydrophobic portions on the active surface of cholinesterase, situated both close to the esterase center and close to the anionic center.
Databáze:	OpenAIRE
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