Brief cold shock given to corn root tissue which has been preloaded with 32P-labeled phosphate increases the phosphorylation of microsomal membrane proteins. Gel electrophoresis shows that discrete proteins are labeled. Preincubation of sealed microsomal vesicles under conditions producing membrane protein phosphorylation causes a 25% loss of total ATPase activity and 55% loss of uncoupler-sensitive activity. It is believed that the effect of injury or shock in blocking H+ efflux pumping by corn roots may be attributed to phosphorylation of the H+-ATPase. Calcium influx attending injury may be responsible for activating the protein kinase.

Inhibition of proton pumping in corn roots is associated with increased phosphorylation of membrane proteins / G. Zocchi, S.A. Rogers, J.B. Hanson. - In: PLANT SCIENCE LETTERS. - ISSN 0304-4211. - 31:2-3(1983 Sep), pp. 215-221.

Inhibition of proton pumping in corn roots is associated with increased phosphorylation of membrane proteins

G. Zocchi
;
1983

Abstract

Brief cold shock given to corn root tissue which has been preloaded with 32P-labeled phosphate increases the phosphorylation of microsomal membrane proteins. Gel electrophoresis shows that discrete proteins are labeled. Preincubation of sealed microsomal vesicles under conditions producing membrane protein phosphorylation causes a 25% loss of total ATPase activity and 55% loss of uncoupler-sensitive activity. It is believed that the effect of injury or shock in blocking H+ efflux pumping by corn roots may be attributed to phosphorylation of the H+-ATPase. Calcium influx attending injury may be responsible for activating the protein kinase.
Calcium; Calmodulin; H+-ATPase; Microsomal membranes; Protein phosphorylation
Settore AGR/13 - Chimica Agraria
set-1983
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/240468
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