Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase

FEBS Letters

Chhajlani, Vijay²  Earles, Betty²  Derr, Dwight²  August, Thomas²  Schmell, Eli¹ 

[1] Molecular Biology Program, The Office of Naval Research, Arlington, VA 22217, USA;Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA

关键词: Acetylcholinesterase;    Immunoaffinity chromatography;    Amino acid sequence;   

DOI  :  10.1016/0014-5793(89)81352-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown