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

Terrone L. Rosenberry; Philip Barnett; Carol Mays

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

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

Terrone L. Rosenberry, Philip Barnett, Carol Mays

Neuroscience

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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.

Original language	English (US)
Pages (from-to)	135-147
Number of pages	13
Journal	Neurochemistry International
Volume	2
Issue number	C
DOIs	https://doi.org/10.1016/0197-0186(80)90020-0
State	Published - 1980

Keywords

Acetylcholinesterase
basement membrane
collagen-like subunits
neuromuscular junction
pepsin-resistant fragments

ASJC Scopus subject areas

Cellular and Molecular Neuroscience
Cell Biology

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10.1016/0197-0186(80)90020-0

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title = "The collagen-like subunits of acetylcholinesterase from the eel electrophorus electricus",

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.",

keywords = "Acetylcholinesterase, basement membrane, collagen-like subunits, neuromuscular junction, pepsin-resistant fragments",

author = "Rosenberry, {Terrone L.} and Philip Barnett and Carol Mays",

year = "1980",

doi = "10.1016/0197-0186(80)90020-0",

language = "English (US)",

volume = "2",

pages = "135--147",

journal = "Neurochemistry International",

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T1 - The collagen-like subunits of acetylcholinesterase from the eel electrophorus electricus

AU - Rosenberry, Terrone L.

AU - Barnett, Philip

AU - Mays, Carol

PY - 1980

Y1 - 1980

N2 - 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.

AB - 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.

KW - Acetylcholinesterase

KW - basement membrane

KW - collagen-like subunits

KW - neuromuscular junction

KW - pepsin-resistant fragments

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U2 - 10.1016/0197-0186(80)90020-0

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SN - 0197-0186

VL - 2

SP - 135

EP - 147

JO - Neurochemistry International

JF - Neurochemistry International

IS - C

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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