Synthesis of an integral protein of the protein-body membrane in Phaseolus vulgaris cotyledons

Planta ◽  
1984 ◽  
Vol 160 (4) ◽  
pp. 330-340 ◽  
Author(s):  
Michael M�der ◽  
Maarten J. Chrispeels
Keyword(s):  
Phaseolus Vulgaris ◽  
Protein Body ◽  
Integral Protein ◽  
Protein Body Membrane

The behavior of ATPase in cotyledon tissue during germination

1972 ◽  
Vol 50 (2) ◽  
pp. 327-332 ◽  
Author(s):  
Y. F. Lai ◽  
J. E. Thompson
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Phaseolus Vulgaris ◽  
Atpase Activity ◽  
Major Part ◽  
Protein Body ◽  
Transport Processes ◽  
Assay Mixture ◽  
Storage Cells ◽  
Soluble Fractions

The behavior of ATPase in cotyledon tissue of Phaseolus vulgaris during germination has been examined with a view to assessing the feasibility of its involvement in transport processes. Both basal ATPase activity (no cations added to the assay mixture) and Na+–K+ stimulated activity were routinely present in homogenates of the tissue but decreased during germination in a manner that corresponded very closely with the pattern of protein attenuation for the same period. Since the decreased levels of protein primarily reflect protein body digestion, this parallel behavior suggests that as the need for transport of metabolites out of the storage cells becomes less, there is a corresponding decrease in the levels of basal and cation-stimulated ATPases.Fractionation of the tissue revealed that ATPase activity is present in isolated soluble fractions, but throughout the germination period the major proportions of both basal and Na+–K+ stimulated activities proved to be particulate and were distributed among nuclear, mitochondrial, and microsomal fractions. Since both types of ATPase are present in purified cell wall and plasma membrane from this tissue, this distribution is thought to reflect in large part fragmentation of cell wall and plasma membrane incurred during homogenization. Thus the subcellular distributions of the enzymes as well as their patterns of change during germination are consistent with the involvement of a major part of the cotyledon ATPase activity in transport phenomena.

Four putative, glyoxysome membrane proteins are instead immunologically-related protein body membrane proteins

Plant Science ◽  
1995 ◽  
Vol 106 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Jeff Bunkelmann ◽  
Francisco J. Corpas ◽  
Richard N. Trelease
Keyword(s):  
Membrane Proteins ◽  
Protein Body ◽  
Related Protein ◽  
Protein Body Membrane

scholarly journals Molecular characterization of proteins in protein-body membrane that disappear most rapidly during transformation of protein bodies into vacuoles

1995 ◽  
Vol 7 (2) ◽  
pp. 235-243 ◽  
Author(s):  
Kaori Inoue ◽  
Asako Motozaki ◽  
Yuka Takeuchi ◽  
Mikio Nishimura ◽  
Ikuko Hara-Nishimura
Keyword(s):  
Molecular Characterization ◽  
Protein Body ◽  
Protein Bodies ◽  
Protein Body Membrane

Different routes for integral protein insertion into Ricinus communis protein-body and glyoxysome membranes

Planta ◽  
1989 ◽  
Vol 179 (3) ◽  
pp. 331-339 ◽  
Author(s):  
Claire Halpin ◽  
Michael J. Conder ◽  
J. Michael Lord
Keyword(s):  
Ricinus Communis ◽  
Protein Body ◽  
Protein Insertion ◽  
Integral Protein

Identification of some major cytokinins in Phaseolus vulgaris and their distribution

1996 ◽  
Vol 96 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Russell D. Hammerton ◽  
Bjorn Nicander ◽  
Elisabeth Tillberg
Keyword(s):  
Phaseolus Vulgaris

Chromium-induced inhibition of ethylene evolution in bean (Phaseolus vulgaris) leaves

1993 ◽  
Vol 89 (2) ◽  
pp. 404-408
Author(s):  
Charlotte Poschenrieder ◽  
Benito Gunse ◽  
Juan Barcelo
Keyword(s):  
Phaseolus Vulgaris ◽  
Ethylene Evolution
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