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Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase
Author(s) -
Chhajlani Vijay,
Derr Dwight,
Earles Betty,
Schmell Eli,
August Thomas
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81352-3
Subject(s) - acetylcholinesterase , torpedo , biochemistry , enzyme , chemistry , peptide sequence , chromatography , amino acid , affinity chromatography , butyrylcholinesterase , cysteine , gene , aché , receptor , acetylcholine receptor
A single step immunoaffinity purification procedure for human erythrocyte acetylcholinesterase is described which permitted the isolation of milligram quantities of enzyme from 10 U of erythrocytes, with 113 000‐fold purification and a yield of about 22%. In SDS‐PAGE analysis, the enzyme corresponds to a disulfide linked dimer of 140 kDa which is converted to a 70 kDa monomer upon disulfide reduction. The tryptic peptides generated from purified enzyme were separated by reverse‐phase HPLC. Five of these peptides were analysed to determine the amino acid sequences. The obtained sequences showed no homology to the already known amino acid sequences for human serum and brain butyryl‐cholinesterase and Torpedo californica acetylcholinesterase.