[Participation of phenylalanine-p-nitroanilidase in the decomposition of reserve proteins of germinating vetch seeds].
L-phenylalanine-p-nitroanilidase (PPA-ase) from vetch cotyledons was purified 1600-fold with a 6.7% recovery. Data from gel electrophoresis suggest that the preparation obtained (specific activity 232 U/mg) contains only a small admixture of inactive protein. PPA-ase splits off more than 14% of peptide bonds of di- and oligopeptides formed by reserve protein hydrolysis with endogenous protease A. The cotyledon PPA-ase is located outside the protein bodies and differs from seedling enzymes hydrolyzing PPA by its chromatographic behaviour. The results obtained suggest that PPA-ase takes part in the hydrolysis of short peptides produced during the reserve protein degradation and transported from protein bodies in the cytoplasm.
D000626:Aminopeptidases / Q000378:metabolism*; D007700:Kinetics; D063245:Plant Development; D018521:Plant Physiological Phenomena; D010940:Plant Proteins / Q000378:metabolism*; D012639:Seeds / Q000378:metabolism
D010940:Plant Proteins; D000626:Aminopeptidases; C038455:phenylalanine p-nitroanilidase
Ob uchastii fenilalanin-p-nitroanilidazy v raspade zapasnykh belkov prorastaiushchikh semian viki.