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PMID: 3129414 Published · ppublish English Journal Article

In vitro conditions for the self-polymerization of the microtubule-associated protein, tau factor.

Journal of biochemistry ·Vol. 102 ·No. 6 ·1987-12-00 ·Pages 1415-21

Montejo de Garcini E, Avila J

Abstract

One of the microtubule associated proteins, tau factor, that appears associated to the paired helical filaments of Alzheimer's disease presents, by itself, after urea treatment, the ability of polymerizing in vitro as tested by immunoelectronmicroscopy. These polymers resemble in their width and appearance those of the paired helical filaments. The conditions required for this assembly have been studied and determined the protein concentration needed, the influence of salt concentration and pH as well as the possible modifications (deamination, acylation) which may be implied in such in vitro polymerization.

MeSH Terms
Alzheimer Disease/metabolism Animals Glutaminase/metabolism Gold Humans Hydrogen-Ion Concentration Immunologic Tests Microscopy, Electron Microtubule-Associated Proteins/metabolism Nerve Tissue Proteins Polymers Protein Conformation Staphylococcal Protein A Swine Urea/pharmacology tau Proteins
Chemicals
Microtubule-Associated Proteins Nerve Tissue Proteins Polymers Staphylococcal Protein A tau Proteins Gold Urea Glutaminase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Montejo de Garcini E
Centro de Biologia Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Avila J
Article Info
Journal
Journal of biochemistry
Abbr.
J Biochem
ISSN
0021-924X
Published
1987-12-00
Pages
1415-21
Language
English
Region
England
NLM ID
0376600
Subset
IM
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