Comparative effects of limited tryptic hydrolysis on physicochemical and structural features of seed 11S globulins.

The effect of the limited proteolysis by trypsin on selected seed storage 11S globulins (broad bean and pea legumins, glycinin and helianthinin) was studied by high-sensitive differential scanning calorimetry, fluorescence spectroscopy and analysis of proteolysis kinetics. Different behaviour of glycinin and helianthinin, on one hand, and broad bean and pea legumins, on the other, were observed: in the first group changes in the physicochemical characteristics of the proteins due to their limited proteolysis are more pronounced in comparison with the second one, in relation with the extent of primary structure modifications. The differences observed have been evaluated in relation with the amino acid sequence features of the four 11S globulin studied and agree with the literature data concerning the protein structural changes in the course of the limited proteolysis.

Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances.

The effect of exogenous and endogenous products storage in lysosomes on the activity and multiple forms of alpha-L-fucosidase from human skin fibroblasts was investigated. It was shown that sucrose load, modelling intralysosomal accumulation of nonhydrolyzable products, causes certain changes in secretion level of alpha-L-fucosidase and multiple forms' spectra of the intracellular and secreted enzymes. These changes were different for the enzyme from embryonal and postnatal normal fibroblasts.

Comparative studies of intracellular activity, secretion and multiple forms spectra of human skin fibroblast alpha-L-fucosidase in the normaland after sucrose load.

Activity and multiple forms of intracellular and secreted alpha-L-fucosidases from human skin fibroblasts were studied in normal and sucrose-loaded cells--modelling intralysosomal nonhydrolyzable products' accumulation in vitro. Certain differences in secretion levels were found after sucrose load for alpha-L-fucosidases from embryonal and postnatal cell lines. Different effects of sucrose load on multiple forms' spectra of the intracellular and secreted alpha-L-fucosidases from embryonal and postnatal fibroblasts were revealed.