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Title: Regulation of protein phosphorylation in oat mitochondria

Abstract

We sought to identify phosphorylated proteins in isolated oat mitocchondria and to characterize the enzymatic and regulatory properties of the protein kinase(s). Mitochondria from oats (Avena sativa L. cv. Garry) were purified on Percoll gradients. Mitochondria were incubated with {sup 32}P-{gamma}-ATP; proteins were separated by SDS-PAGE. A small number of bands was detected on autoradiograms, most prominently at 70 kD and 42 kD; the latter band has been tentatively identified as a subunit of the pyruvate dehydrogenase complex, a well-known phosphoprotein. The protein kinase(s) could also phosphorylate casein, but not histone. Spermine enhanced the phosphorylation of casein and inhibited the phosphorylation of the 42 kD band. These studies were carried out on both intact and burst mitochondria. Control by calcium and other ions was investigated. The question of the action of regulators on protein kinase or protein phosphatase was studied by the use of {sup 35}S-adenosine thiotriphosphate.

Authors:
; ;  [1]
  1. Franklin and Marshall College, Lancaster, PA (USA)
Publication Date:
OSTI Identifier:
6611066
Resource Type:
Journal Article
Journal Name:
Plant Physiology, Supplement; (USA)
Additional Journal Information:
Journal Volume: 89:4; Journal ID: ISSN 0079-2241
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PHOSPHOTRANSFERASES; CHEMICAL COMPOSITION; PROTEINS; PHOSPHORYLATION; ATP; AUTORADIOGRAPHY; CASEIN; MITOCHONDRIA; OATS; PHOSPHORUS 32; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CELL CONSTITUENTS; CEREALS; CHEMICAL REACTIONS; DAYS LIVING RADIOISOTOPES; ENZYMES; GRASS; ISOTOPES; LIGHT NUCLEI; LILIOPSIDA; MAGNOLIOPHYTA; NUCLEI; NUCLEOTIDES; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANIC PHOSPHORUS COMPOUNDS; ORGANOIDS; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; PLANTS; RADIOISOTOPES; TRANSFERASES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Pike, C, Kopeck, K, and Sceppa, E. Regulation of protein phosphorylation in oat mitochondria. United States: N. p., 1989. Web.
Pike, C, Kopeck, K, & Sceppa, E. Regulation of protein phosphorylation in oat mitochondria. United States.
Pike, C, Kopeck, K, and Sceppa, E. 1989. "Regulation of protein phosphorylation in oat mitochondria". United States.
@article{osti_6611066,
title = {Regulation of protein phosphorylation in oat mitochondria},
author = {Pike, C and Kopeck, K and Sceppa, E},
abstractNote = {We sought to identify phosphorylated proteins in isolated oat mitocchondria and to characterize the enzymatic and regulatory properties of the protein kinase(s). Mitochondria from oats (Avena sativa L. cv. Garry) were purified on Percoll gradients. Mitochondria were incubated with {sup 32}P-{gamma}-ATP; proteins were separated by SDS-PAGE. A small number of bands was detected on autoradiograms, most prominently at 70 kD and 42 kD; the latter band has been tentatively identified as a subunit of the pyruvate dehydrogenase complex, a well-known phosphoprotein. The protein kinase(s) could also phosphorylate casein, but not histone. Spermine enhanced the phosphorylation of casein and inhibited the phosphorylation of the 42 kD band. These studies were carried out on both intact and burst mitochondria. Control by calcium and other ions was investigated. The question of the action of regulators on protein kinase or protein phosphatase was studied by the use of {sup 35}S-adenosine thiotriphosphate.},
doi = {},
url = {https://www.osti.gov/biblio/6611066}, journal = {Plant Physiology, Supplement; (USA)},
issn = {0079-2241},
number = ,
volume = 89:4,
place = {United States},
year = {Sat Apr 01 00:00:00 EST 1989},
month = {Sat Apr 01 00:00:00 EST 1989}
}