Acylated arachins. Physicochemical properties.
Acetylated and succinylated arachins were examined for various physico-chemical parameters such as viscosity, absorption and fluorescence spectra, gel electrophoretic patterns, gel filtration profiles and susceptibility to proteolysis. Acetylation and succinylation lead to dissociation of arachin into lower molecular weight fractions. The lower molecular weight fractions had a higher degree of succinylation compared to other fractions. The absorption and the fluorescence spectra were perturbed both by acetylation and by succinylation. Both fluorescence and viscosity data indicate denaturation of acylated arachins. The modified arachin was more susceptible to proteolysis by trypsin and chymotrypsin and varied in degree of hydrolysis.
D000215:Acylation; D004591:Electrophoresis, Polyacrylamide Gel; D010940:Plant Proteins; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014783:Viscosity
D010940:Plant Proteins; C000102:Arachin