[Detection and study of a protein factor mediating stimulation of disulfide reductase activity by cyclic 3', 5'-AMP and other effectors].

DSR stimulation in the supernatant fraction under the effect of 3', 5'-AMP 10(-7) M, ATP 5.10(-5) M, Mg2+5.10(-5) M, EDTA 5.10(-4) M and protamine 5 mg/ml was mediated through a factor which was readily sorbed by BaSO4, Al (OH)3 and activated carbon, and was easily eluated with a 10-fold increase of the buffer molarity. Barium eluates of the liver and of the brain restored the effect of 3', 5'-AMP eliminated by BaSO4, crosswise and equally. Apparently, the sorbed factor was a protein since it was not dialyzed, very thermolabile and readily inactivated by a low trypsin concentrations. The factor restored the DSR activation eliminated or decreased by the protein proteinkinase inhibitor (PPKI). A linear relationship between active quantities of the PPKI and the protein factor were in favour of the fact that the protein factor was affiliated or identical to proteinkinase. A possible biological significance of the DSR activation and the hypothesis on the existence of a special protamine-sensitive proteinkinase is discussed.