Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine
- 1 January 1976
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 131 (1) , 81-86
- https://doi.org/10.1007/bf00387349
Abstract
Cotyledonary cells are submitted to fractionation by isopycnic centrifugation. Small intact protein bodies are collected in the densest zones (d=1.205–1.237 g/cm3). Fragments of larger bodies are gathered in zones of lower density (d=1.205 g/cm3). Small dense bodies are largely sedimentable after dilution, whereas fragments of the large bodies dissociate into a dense sedimentable clot and into floating elements which contain most of the globulins and all of the albumins. Among the dissociated floating components are the BAPA-active endopeptidases and the trypsin inhibitors (BAPA=α-N-benzoyl-DL-arginine-p-nitroanilide). A caseolytic activity remains with the dense mass. The localisation of the albumins, globulins, proteases and trypsin inhibitors is discussed. Relations between solubility, structure and function are considered.This publication has 7 references indexed in Scilit:
- Isolation and Analysis of Protein Bodies from Cotyledons ofLablab purpureusandPhaseolus vulgaris(Leguminoseae)Physiologia Plantarum, 1976
- Activites proteolytiques et anti-trypsine des graines de Vigna unguiculata: Repartition et interactionPhytochemistry, 1975
- The Lytic Compartment of Plant CellsPublished by Springer Nature ,1975
- Inhibiteurs anti-trypsine et activités protéolytiques des Albumines de graine de Vigna unguiculataPlanta, 1974
- Localization and activity of various peptidases in germinating barleyPlanta, 1972
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951