来自电鳗（电鳐）的乙酰胆碱酯酶的类胶原蛋白亚基。

The collagen-like subunits of acetylcholinesterase from the eel electrophorus electricus.

作者信息

Rosenberry T L, Barnett P, Mays C

机构信息

The Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106 USA; the Department of Neurology, Columbia University, New York, New York 10032 USA.

出版信息

Neurochem Int. 1980;2C:135-47. doi: 10.1016/0197-0186(80)90020-0.

DOI:10.1016/0197-0186(80)90020-0

PMID:20487779

Abstract

Pepsin-resistant fragments of the tail subunits of 14S and 18S acetylcholinesterase from eel electric organ have been isolated and characterized. The native fragments are composed of three 24,000 molecular weight polypeptides linked by intersubunit disulfide bonds in a collagen-like triple helix. Intact tail subunits have also been isolated. These subunits appear to contain both the triple-helical domain and a noncollagenous domain that is linked to catalytic subunits by disulfide bonds.

摘要

已分离并鉴定了来自电鳗电器官的14S和18S乙酰胆碱酯酶尾部亚基的胃蛋白酶抗性片段。天然片段由三个分子量为24,000的多肽组成，这些多肽通过亚基间二硫键以类胶原三螺旋形式相连。完整的尾部亚基也已被分离出来。这些亚基似乎同时包含三螺旋结构域和一个通过二硫键与催化亚基相连的非胶原结构域。