Search results for "Protein body"
showing 2 items of 2 documents
Intracellular localisation of some peptidases and alpha-mannosidase in cotyledons of resting kidney bean, Phaseolus vulgaris
1986
Cotyledons of resting kidney beans (Phaseolus vulgaris, L., cv. “Processor”) contain high activities of two alkaline peptidases, an aminopeptidase (EC 3.4.11) acting on Leu-Tyr and Leu-Gly-Gly and a dipeptidase (EC 3.4.13) hydrolysing Ala-Gly together with low activities of neutral naphthyiamidases (marker substrate Leu-β-NA) and of acid carboxypeptidases (EC 3.4.16; marker substrate Z-Phe-Ala). The intracellular localisation of these peptidases and that of α-mannosidase (EC 3.2.1.24) was studied by subcellular fractionations in different media. In density gradient centrifugations in non-aqueous glycerol-potassium iodide media the alkaline peptidases remained mainly in the application zone …
Ultrastructural Studies on Development in Mature Seeds; Embryos ofEuonymus europaeaL. Dormant or Cultured at +25 °C
1989
Ultrastructural observations on naturally dispersed and dehydrated seeds of Euonymus europaea L. were performed. It was shown that during the culture of isolated embryos at 25 °C for 7 d the maturation of protein bodies continued; the initial juvenile form (single protein body per cell with dispersed contents) was developing into a more advanced form (single body split to form several sub-units with condensed contents). Parallel biochemical determinations pointed to an increase in insoluble protein levels. There were no changes in other storage organelles, lipid bodies, either in the fine structure or in the level of triacylglycerols. Deterioration of cellular membranes (in mitochondria, pr…