Universal isolation of cross-linked peptides: Application to neurofibrillary tangles

被引：5

作者：

Chen, XH ^{[1
]}

Eswaran, D ^{[1
]}

Smith, MA ^{[1
]}

Perry, G ^{[1
]}

Anderson, VE ^{[1
]}

机构：

[1] Case Western Reserve Univ, Dept Biochem, Cleveland, OH 44106 USA

来源：

BIOCONJUGATE CHEMISTRY | 1999年 / 10卷 / 01期

关键词：

D O I：

10.1021/bc980098v

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A universal procedure to isolate cross-linked peptides has been demonstrated. The procedure relies on initially converting the E-amino groups of lysine to dimethyl lysine by reductive methylation with sodium cyanoborohydride and formaldehyde. The lysine-modified protein is proteolytically cleaved and the resulting cl-amino groups derivatized with methoxypoly(ethylene glycol)(5000) succinyl hydroxy-succinimide. Any unintentional derivatization of tyrosine side chains can be reversed by incubation under mildly alkaline conditions. The cross-linked polypeptides contain two poly(ethylene glycol)(5000) chains while non-cross-linked peptides contain a single poly(ethylene glycol)(5000) chain. The two populations of peptides can be separated by gel filtration chromatography. This procedure has been shown capable of isolating cross-linked peptides using glutathione, lysozyme, chemically cross-linked hemoglobin, and neurofibrillary tangles isolated from the brain of a case of Alzheimer's disease.

引用

页码：112 / 118

页数：7

共 23 条

[1]

CATLEY BJ, 1969, J BIOL CHEM, V244, P933

[2] RNA-POLYMERASE-II FROM WHEAT-GERM - A CROSS-LINKING STUDY OF SUBUNITS TOPOGRAPHY [J].

CERVONI, L ;

FERRARO, A ;

GIARTOSIO, A ;

WANG, CQ ;

TURANO, C .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1994, 311 (01) :35-41

[3] Probing protein folding and stability using disulfide bonds [J].

Darby, N ;

Creighton, TE .

MOLECULAR BIOTECHNOLOGY, 1997, 7 (01) :57-77

[4]

Darby N, 1995, Methods Mol Biol, V40, P219

[5] Mapping the mechanism-based modification sites in L-aspartase from Escherichia coli [J].

Giorgianni, F ;

Beranova, S ;

Wesdemiotis, C ;

Viola, RE .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1997, 341 (02) :329-336

[6] COVALENT PROTEIN CROSS-LINKS - GENERAL DETECTION, QUANTITATION, AND CHARACTERIZATION VIA MODIFICATION WITH DIPHENYLBORINIC ACID [J].

GRAHAM, L ;

GALLOP, PM .

ANALYTICAL BIOCHEMISTRY, 1994, 217 (02) :298-305

[7]

JENTOFT N, 1983, METHOD ENZYMOL, V91, P570

[8] MODIFICATION OF HUMAN HEMOGLOBIN WITH METHYL ACYL PHOSPHATES DERIVED FROM DICARBOXYLIC-ACIDS - SYSTEMATIC RELATIONSHIPS BETWEEN CROSS-LINKED STRUCTURE AND OXYGEN-BINDING PROPERTIES [J].

JONES, RT ;

HEAD, CG ;

FUJITA, TS ;

SHIH, DTB ;

WODZINSKA, J ;

KLUGER, R .

BIOCHEMISTRY, 1993, 32 (01) :215-223

[9] DETERMINATION OF THE RELATIVE POSITIONS OF AMINO-ACIDS BY PARTIAL SPECIFIC CLEAVAGES OF END-LABELED PROTEINS [J].

JUE, RA ;

DOOLITTLE, RF .

BIOCHEMISTRY, 1985, 24 (01) :162-170

[10] 3-POINT CROSS-LINKING - POTENTIAL RED-CELL SUBSTITUTES FROM THE REACTION OF TRIMESOYL TRIS(METHYL PHOSPHATE) WITH HEMOGLOBIN [J].

KLUGER, R ;

WODZINSKA, J ;

JONES, RT ;

HEAD, C ;

FUJITA, TS ;

SHIH, DT .

BIOCHEMISTRY, 1992, 31 (33) :7551-7559

← 1 2 3 →