An influence of stress protein CSP 310 and antiserum against this protein on lipid peroxidation in cereal mitochondria.
It is determined that an addition of an anti-CSP 310 antiserum to isolated winter wheat and maize mitochondria caused more significant increasing of spontaneous lipid peroxidation than the addition of stress protein CSP 310. It is shown that, at function of different mitochondrial respiratory chain complexes, the lipid peroxidation in winter wheat and maize mitochondria take place with different intensities. Under the functioning of mitochondrial respiratory chain complex IV, the maximum output of lipid peroxidation products, dienic conjugates is detected. The presence of antiserum against CSP 310 in incubation media induces lipid peroxidation more than the presence of CSP 310 in mitochondria isolated from stressed plants under these conditions. Based on data obtained, it is possible to conclude that in vivo endogenous CSP 310, during a cold stress, has an antioxidant activity the same as other known uncoupling proteins.
Kolesnichenko
A V
AV
Siberian Institute of Plant Physiology and Biochemistry, Siberian Division of Russian Academy of Sciences, Irkutsk.
Grabelnych
O I
OI
Tourchaninova
V V
VV
Zykova
V V
VV
Koroleva
N A
NA
Pobezhimova
T P
TP
Voinikov
V K
VK
D002352:Carrier Proteins / Q000276:immunology / Q000378:metabolism / Q000502:physiology*; D004579:Electron Transport; D007106:Immune Sera; D007473:Ion Channels; D015227:Lipid Peroxidation / Q000276:immunology*; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism / Q000502:physiology*; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D014908:Triticum / Q000378:metabolism*; D000071256:Uncoupling Protein 1
D002352:Carrier Proteins; D007106:Immune Sera; D007473:Ion Channels; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D000071256:Uncoupling Protein 1