Separation of hydrolytically active components of cellulase from Myrothecium verrucaria by starch gel electrophoresis
conference paper
Using starch gel electrophoresis according to Smithies, desalted crude cellulase from Myrothecium verrucqria was separated into at least 12 protein zones. These were tested on their activity towards p-nitrophenyl-β-D-glucoside, sodium carboxymethylcellulose and α-cellulose. They were all hydrolytically active.
When the separate proteins were subjected to re-electrophoresis, they appeared at the same position as that, at which they appeared upon electrophoresis of the crude preparation. In some of the protein zones reducing sugars were found. The results obtained are indicative of a multiple nature of the cellulase from M. verrucaria, but are not contradictory to the conception that one, or a limited number of proteins, would be associated with other substances, thus yielding conjugated proteins with different physical and enzymatic properties.
When the separate proteins were subjected to re-electrophoresis, they appeared at the same position as that, at which they appeared upon electrophoresis of the crude preparation. In some of the protein zones reducing sugars were found. The results obtained are indicative of a multiple nature of the cellulase from M. verrucaria, but are not contradictory to the conception that one, or a limited number of proteins, would be associated with other substances, thus yielding conjugated proteins with different physical and enzymatic properties.
TNO Identifier
283149
Source title
Proceedings 5th international symposium Chromatographie-Electrophorèse
Pages
242-255