An influence of antiserum against winter wheat stress uncoupling protein, CSP 310, on energetic activity of some plant species mitochondria.

It is determined that addition of an anti-CSP 310 antiserum to isolated mitochondria of cereals (winter rye, winter wheat, and maize) caused an increasing of mitochondrial respiratory control. In a similar manner, addition of this antiserum to isolated pea mitochondria did not cause this effect. It is shown that coupling effect of antiserum is not dependent upon the presence of bovine serum albumin in mitochondria incubation media. Therefore, these results show that the mechanism of oxidation and phosphorylation uncoupling, and participation of immunochemically related CSP 310 proteins that can be precipitated by anti-CSP 310 antiserum is specific for cereals.

The search for proteins with immunochemical affinity to plant stress proteins at cold-adapted endemic Baikal fishes.

The search for proteins with immunochemical affinity to plant stress proteins in endemic Baikal fishes shows the presence of proteins, immunochemically related to plant heat-stabile proteins and plant uncoupling protein CSP 310. Western blotting showed that among the native cytoplasmic proteins of endemic Baikal fishes there are proteins immunochemically related to heat-stabile plant proteins with molecular weights about 480, 200-290, 150, 140 and about 90-100kD. SDS-electrophoresis showed the presence of polypeptides with molecular weights 23, 17 and 14kD in all species investigated and an additional 35kD polypeptide in Cottocomephorus grewingki. The search for polypeptides with immunochemical affinity to plant stress uncoupling protein CSP 310 in endemic Baikal fishes shows the presence of a 14kD polypeptide, immunochemically related to it.