The aim of the diploma thesis was to assess changes in pattern of legume storage proteins during germination. Four species of legumes were chosen for analyses ? Glycine max L., Lupinus angustifolius L., Pisum sativum L. and Vicia faba L. Seeds for analyses were sampled at the beginning, middle and end of germination. Proteins were extracted from lyophilised and homogenised material. These proteins were analysed by SDS-PAGE electrophoresis. The results proved that during seed germination the seed storage proteins cleave into smaller peptides, which forms new proteins. The intensity of protein bands in pea seeds was decreased in the area at around 48-45 kda and 40-36 kDa and the intensity of the proteins bands was increased at around the protein bands 25-23 kDa and 19-7 kDa. In lupine were not detected the protein bands over 39 kDa and during germination amount of protein bands in areas 15-7 kDa was increased

Humans have two plasminogen activators (PAs), tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), which generate plasmin to breakdown fibrin and other barriers to cell migration. Both PAs are used as pharmaceuticals but their efficacies are limited by their rapid clearance from the circulation, predominantly by parenchymal cells of the liver. At the commencement of the work presented here, the hepatic receptors responsible for mediating the catabolism of the PAs were little understood. tPA degradation by hepatic cell lines was known to depend on the formation of binary complexes with the major PA inhibitor, plasminogen activator inhibitor type-1 (PAI-1). Initial studies presented here established that uPA was catabolised in a fashion similar to tPA by the hepatoma cell line, HepG2. Other laboratories around this time found that the major receptor mediating the binding and endocytosis of the PAs is Low Density Lipoprotein Receptor-related Protein (LRP1). LRP1 is a giant 600 kDa protein that binds a range of structurally and functionally diverse ligands including, activated α2 macroglobulin, apolipoproteins, β amyloid precursor protein, and a number of serpin-enzymes complexes, including PA??PAI-1 complexes. Further studies for the work presented here centred on this receptor. By using radiolabelled binding assays, ligand blots, and Western blots on cultured cells, the major findings are that: (1) basal LRP1 expression on HepG2 is low compared to a clone termed, HepG2a16, but appears to increase in long term culture; (2) a soluble form of LRP1, which retains ligand-binding capacity, is present in human circulation; (3) soluble LRP1 is also present in cerebral spinal fluid where its role in neurological disorders such as Alzheimer??s disease is a developing area of interest; and (4) the release of LRP1 is a mechanism conserved in evolution, possibly as distantly as molluscs. The discovery, identification, and characterisation of soluble LRP1 introduces this protein in the human circulation, and presents a possible further level of regulation for its associated receptor system.