On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: ## 11. Peptide sequence analysis The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in "stainability" of different proteins. Despite efforts
On the relationship of amino acid composition to silver staining of proteins in electrphoresis gels
β Scribed by Dr. Douglas M. Gersten; Pamela H. Wolf; Robert S. Ledley; Lewis V. Rodriguez; Edward J. Zapolski
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 570 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0173-0835
No coin nor oath required. For personal study only.
β¦ Synopsis
On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels
Development of techniques for silver staining of proteins separated by polyacrylamide gel electrophoresis has increased experimental detection limits. However, the precise basis for the reaction between silver and polypeptides is still unclear and, depending upon the choice of silver reagent, may even differ. We compared protein stain intensity with silver diamine (ammoniacal silver) and silver nitrate reagents based on amino acid composition by determining the protein amount required to generate an arbitrary staining intensity and then calculating moles ofeach amino acid present in some representative proteins. W e compared these values for each amino acid, taken singly, as well as for combinations oftwo and more. In no case could staining be attributed entirely to specific or classes of amino acids, thus supporting the argument that an inherent difference exists between primary reactive centers for the two staining reagents.
π SIMILAR VOLUMES
A method has been developed for determination of the specific radioactivity of t-leucine in different proteins or protein subunits which have been separated by polyacrylamide gel electrophoresis. After electrophoresis, the proteins are visualized by staining with Coomassie Brilliant Blue R, and the