MODIFIED AMYLOID-BETA PROTEIN ENDING AT 42 OR 40 WITH DIFFERENT SOLUBILITY ACCUMULATES IN THE BRAIN OF ALZHEIMERS-DISEASE

被引：52

作者：

HARIGAYA, Y

SHOJI, M

KAWARABAYASHI, T

KANAI, M

NAKAMURA, T

IIZUKA, T

IGETA, Y

SAIDO, TC

SAHARA, N

MORI, H

HIRAI, S

机构：

[1] GUNMA UNIV,SCH MED,DEPT NEUROL,MAEBASHI,GUMMA 371,JAPAN

[2] TOKYO METROPOLITAN INST MED SCI,DEPT MOLEC BIOL,BUNKYO KU,TOKYO 113,JAPAN

[3] TOKYO INST PSYCHIAT,DEPT MOLEC BIOL,SETAGAYA KU,TOKYO 156,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 211卷 / 03期

关键词：

D O I：

10.1006/bbrc.1995.1912

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Serial extraction study of Alzheimer's disease (AD) and control brains revealed 4, 3.7 and 3 kD amyloid beta protein (A beta) species accumulated in AD brains. In the fractions extracted with TBS, 10% SDS and formic acid, considerable amounts of A beta species were recovered in SDS fractions besides TBS and formic acid tractions. Immunoblotting with several site-specific antibodies confirmed not only the presence of 4 kD A beta starting at the first amino acid of A beta but also 2 smaller A beta species with modification of their amino-termini in the highly resolutional Tris/Tricine gel system. A beta solubility using these solvents was associated with both modification of the amino-terminus and length of carboxyl-terminus of A beta. Especially, a large amount of modified A beta was found to be accumulated as forms with different solubility in AD brains. (C) 1995 Academic Press, Inc.

引用

页码：1015 / 1022

页数：8

共 24 条

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