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Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors
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/cm(3)). Fragments of larger bodies are gathered in zones of lower density (d=1.205 g/cm(3)). Small dense bodies are largely sedimentable afte...
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Published in: | Planta 1976-01, Vol.131 (1), p.81-86 |
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Main Authors: | , , , , |
Format: | Article |
Language: | fre |
Online Access: | Get full text |
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Summary: | 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/cm(3)). Fragments of larger bodies are gathered in zones of lower density (d=1.205 g/cm(3)). 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. |
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ISSN: | 0032-0935 |
DOI: | 10.1007/BF00387349 |