ON THE RELATIONSHIP OF AMINO-ACID-COMPOSITION TO SILVER STAINING OF PROTEINS IN ELECTROPHORESIS GELS .2. PEPTIDE SEQUENCE-ANALYSIS

被引:10
作者
GERSTEN, DM
RODRIGUEZ, LV
GEORGE, DG
JOHNSTON, DA
ZAPOLSKI, EJ
机构
[1] UNIV TEXAS,MD ANDERSON CANCER CTR,DEPT MOLEC PATHOL,HOUSTON,TX 77030
[2] GEORGETOWN UNIV,MED CTR,NATL BIOMED RES FDN,WASHINGTON,DC 20007
[3] UNIV TEXAS,MD ANDERSON CANCER CTR,DEPT BIOMATH,HOUSTON,TX 77030
[4] NIH,DIV RES GRANTS,BETHESDA,MD 20892
关键词
D O I
10.1002/elps.1150120605
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in "stainability" of different proteins. Despite efforts by many researchers, the precise basis of the reaction between silver reagents and polypeptides is still unclear, and, depending on the formulation, may even differ. We have tested the hypothesis that differences in stainability among proteins can be attributed to differences in di- or tripeptide composition. The results indicate that some order of protein structure other than short peptides accounts for the staining differences observed.
引用
收藏
页码:409 / 414
页数:6
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