English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Affinity-directed cross-linking of membrane-bound acetylcholine receptor polypeptides with photolabile alpha-bungarotoxin derivatives

Witzemann, V., Muchmore, D., & Raftery, M. A. (1979). Affinity-directed cross-linking of membrane-bound acetylcholine receptor polypeptides with photolabile alpha-bungarotoxin derivatives. Biochemistry, 18(24), 5511-5518. doi:10.1021/bi00591a039.

Item is

Files

show Files
hide Files
:
Biochem_18_1979_5511.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
Biochem_18_1979_5511.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Witzemann, Veit1, 2, 3, 4, Author           
Muchmore, D., Author
Raftery, Michael A., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
3Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              
4Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

Content

show
hide
Free keywords: -
 Abstract: Photolabile derivatives of [125I]-alpha-bungarotoxin that retain specific binding to Torpedo californica acetylcholine receptor have been utilized as structural probes of the receptor complex of polypeptide components in its membrane−associated form. The derivatized toxins contained aryl azide side chains poised to form covalent cross-links to both associated and adjacent polypeptides following toxin-receptor complex formation. The results demonstrate that, depending on the possible radius of extension of the photoactivated group from the parent toxin, either (1) both the polypeptide to which the toxin derivative binds and an adjacent polypeptide can be derivatized upon photolysis or (2) only the adjacent polypeptide is labeled. The results lend strong support to the notion that the nicotinic receptor from T. california is composed of a complex of different polypeptides

Details

show
hide
Language(s): eng - English
 Dates: 197919791979-11-27
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 18 (24) Sequence Number: - Start / End Page: 5511 - 5518 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103