Miège Marie-Noëlle, Mascherpa Jean-Michel
Institut de Botanique Systematique et de Biogéographie de l'Université de Genève, Laboratoire de Chimie-Taxonomique, 1, chemin de l'Impératrice CH-1292 - Chambesy (Suisse).
Physiol Plant. 1976 Jul;37(3):229-238. doi: 10.1111/j.1399-3054.1976.tb03963.x.
Protein bodies, isolated by differential and isopycnic centrifugation, have been observed in transmission and scanning electron microscope and biochemically analysed. The powders of the axes and of the cotyledons contain numerous protein bodies, which in the scanning microscope appear to be surrounded by a more or less torn membrane. The proportion of intact, isolated protein bodies is influenced by the grinding methods, but even in the best conditions soaking disaggregates the majority of them. After isopycnic centrifugation, their debris gather in different density zones. Analyses of each zone have revealed that the caseinases are associated with particles of higher density than are peptidases and trypsin inhibitors. A minority population of small-size protein bodies resists the homogenization and fractioning modalities. A double origin of the protein bodies is considered.
