CHARACTERIZATION AND QUANTIFICATION OF MINK SERUM AMYLOID-A PROTEIN USING 2-DIMENSIONAL ELECTROPHORESIS WITH IMMOBILIZED PH GRADIENTS

被引：10

作者：

BRUUN, CF ^{[1
]}

SLETTEN, K ^{[1
]}

HUSBY, G ^{[1
]}

MARHAUG, G ^{[1
]}

机构：

[1] UNIV OSLO,CTR BIOTECHNOL,DEPT BIOCHEM,OSLO,NORWAY

来源：

ELECTROPHORESIS | 1993年 / 14卷 / 12期

关键词：

D O I：

10.1002/elps.11501401211

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Using hydrophobic interaction chromatography, two-dimensional electrophoresis with an immobilized pH gradient in the first dimension and semidry blotting, three isoforms of mink serum amyloid A protein (SAA) were characterized and studied during chronic inflammation. Compared to conventional methods that have been applied to SAA, the major advantages of the present combination of methods are: (i) use of small serum volumes, (ii) rapid extraction, (iii) high resolution, and (iv) high yield of proteins.

引用

页码：1372 / 1374

页数：3

共 14 条

[1]

BURGESS, 1992, APPL THEOR ELECTROPH, V3, P41

[2]

GORG A, 1993, BIOCHEM SOC T, V21, P130

[3] THE CURRENT STATE OF TWO-DIMENSIONAL ELECTROPHORESIS WITH IMMOBILIZED PH GRADIENTS [J].