A study on the degradation of arachin by proteolytic enzymes
Canadian Journal of Botany1973Vol. 51(11), pp. 2217–2222
Abstract
The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.
Related Papers
- Comparison of Surface Modification of Wool Fibres Using Pronase, Trypsin, Papain and Pepsin(2008)
- → On the Agglutinogens of Red Cells Developed with Proteolytic Enzymes and Neuraminidase(1976)5 cited
- → Properties of staphylococcal enterotoxin a under limited protolysis(1982)6 cited
- The Effect of Different Proteolytic Enzymes on the Dissolution of the Zona Pellucida of In vitro Produced Buffalo (Bubalus Bubalis) Embryos(2010)
- → On the Topography of Photoreceptor Membranes(1974)