MOLECULAR PROPERTIES OF ACETYLCHOLINESTERASE

被引：122

作者：

LEUZINGE.W

GOLDBERG, M

CAUVIN, E

机构：

[1] Departments of Biochemistry, Neurology College of Physicians, Surgeons Columbia University, New York, NY

[2] Service de Biochimie Cellulaire, Institut Pasteur, Paris

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1969年 / 40卷 / 02期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0022-2836(69)90470-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The molecular weight of acetylcholinesterase (acetylcholine hydrolase, E.C. 3.1.1.7) has been determined by sedimentation equilibrium and found to be 260,000. The enzyme is split in the presence of guanidine and mercaptoethanol into four subunits, each having one fourth of the molecular weight of the native enzyme. Examination of the C-terminal residues by two independent methods, namely hydrazinolysis and enzymic hydrolysis by carboxypeptidase A, revealed that there are two types of polypeptide chains in acetylcholinesterase. This suggests that acetylcholinesterase has a dimeric hybrid structure, with two α and two β chains. © 1969.

引用

页码：217 / &

共 26 条

[1] KINETICS OF HYDRAZINOLYSIS OF SIMPLE PEPTIDES IN ANHYDROUS HYDRAZINE [J].