Abstract
Human ribonucleases were purified from the sera of Hodgkin's disease patients by sequential column chromatography. The purified enzyme interacted with reverse transcriptase of Rauscher leukemia virus and formed an additive complex of Mr = 130,000. RNase and oligo(dG)-directed reverse transcriptase activities were diminished in the complex. The complex could be dissociated with the subsequent restoration of both activities in the presence of spermidine. The molecular weight of the complex suggest that the 2 RNase molecules bind to a single reverse transcriptase molecule.
Highlights
Human ribonucleases were purified from the sera of Hodgkin’s disease patients by sequential column chromatography
To determine whether a more definitive relationship might exist between the change in RNase activity in the cancer state and the presence of oncornaviral information, we have elected to compare the activities of purified human ribonucleases obtained from six individuals with and without Hodgkin’s disease
100 column chromatography or glycerol gradient centrifugation, the enzymes yielded a single peak of activity without further purification
Summary
Human ribonucleases were purified from the sera of Hodgkin’s disease patients by sequential column chromatography. The arrows at the top of the panel indicate the peak of enzyme activity for either reverse transcriptase (RT) or RNase when each was run separately in the gradient, In panel A, [3HITMP incorporation is shown, in panel B, RNase activity, on the contrary, was stimulated considerably in the presence of spermidine, both in 20 to 28 and in the heavier fractions, 8 to 12, consisting of the complex between the reverse transcriptase and RNase.
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