Trichloroacetic acid treatment as a tricky way for rapid purification of 1N/4R tau protein

被引：6

作者：

Asadollahi, Kazem ^{[1
]}

Rafiee, Saharnaz ^{[1
]}

Riazi, Gholam Hossein ^{[1
]}

Pooyan, Shahriar ^{[1
]}

Afrasiabi, Ali ^{[1
]}

机构：

[1] Univ Tehran, IBB, Tehran, Iran

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2016年 / 118卷

关键词：

4R/1N tau; Protein purification; Trichloroacetic acid; Perchloric acid; Differential precipitation; Heat treatment; PAIRED HELICAL FILAMENTS; IN-VITRO; ALZHEIMERS-DISEASE; AGGREGATION; DNA; PHOSPHORYLATION; MICROTUBULES; POLYMERIZATION; STABILIZATION; GLYCOSYLATION;

D O I：

10.1016/j.pep.2015.10.007

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Tau protein consists of six different isoforms and each one has particular physiological roles. In order to analyze the specific function of each single isoforms, large quantity of highly purified tau isoforms is essential. Many studies have been done to purify tau isoforms by heat treatment, followed by perchloric acid and glycerol precipitation. We found out that 1N/4R tau is soluble in glycerol, that is why mentioned methods do not work for purifying this isoform. In this study, large amounts of active and highly purified (97%) 1N/4R tau protein has been prepared by utilization of trichloroacetic acid as precipitating agent. (C) 2015 Elsevier Inc. All rights reserved.

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页码：98 / 104

页数：7

相关论文

共 61 条

[1] Three Repeat Isoforms of Tau Inhibit Assembly of Four Repeat Tau Filaments [J].

Adams, Stephanie J. ;

DeTure, Michael A. ;

McBride, Melinda ;

Dickson, Dennis W. ;

Petrucelli, Leonard .

PLOS ONE, 2010, 5 (05)

[2] Trichloroacetic acid and trifluoroacetic acid-induced unfolding of cytochrome c:: stabilization of a native-like folded intermediate [J].

Ahmad, A ;

Madhusudanan, KP ;

Bhakuni, V .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 2000, 1480 (1-2) :201-210

[3] Abnormal phosphorylation of tan and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau [J].

Alonso, AD ;

GrundkeIqbal, I ;

Barra, HS ;

Iqbal, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (01) :298-303

[4] ROLE OF ABNORMALLY PHOSPHORYLATED TAN IN THE BREAKDOWN OF MICROTUBULES IN ALZHEIMER-DISEASE [J].

ALONSO, AD ;

ZAIDI, T ;

GRUNDKEIQBAL, I ;

IQBAL, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (12) :5562-5566

[5] Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins [J].

Arnau, Jos ;

Lauritzen, Conni ;

Petersen, Gitte E. ;

Pedersen, John .

PROTEIN EXPRESSION AND PURIFICATION, 2006, 48 (01) :1-13

[6] Disease-related modifications in tau affect the interaction between Fyn and tau [J].

Bhaskar, K ;

Yen, SH ;

Lee, G .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (42) :35119-35125

[7]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[8] Tau protein isoforms, phosphorylation and role in neurodegenerative disorders [J].

Buée, L ;

Bussière, T ;

Buée-Scherrer, V ;

Delacourte, A ;

Hof, PR .

BRAIN RESEARCH REVIEWS, 2000, 33 (01) :95-130

[9] Tau Protein Provides DNA with Thermodynamic and Structural Features which are Similar to those Found in Histone-DNA Complex [J].

Camero, Sergio ;

Benitez, Maria J. ;

Barrantes, Alejandro ;

Ayuso, Jose M. ;

Cuadros, Raquel ;

Avila, Jesus ;

Jimenez, Juan S. .

JOURNAL OF ALZHEIMERS DISEASE, 2014, 39 (03) :649-660

[10] A general method of protein purification for recombinant unstructured non-acidic proteins [J].

Campos, Francisco ;

Guillen, Gabriel ;

Reyes, Jose L. ;

Covarrubias, Alejandra A. .

PROTEIN EXPRESSION AND PURIFICATION, 2011, 80 (01) :47-51

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