Search PubMed⌕ Search

Biomedical subjects

T P Karpetsky

Publications and source records attributed to T P Karpetsky.

8 recordsLinked to original sources
PubMed1979

Ribonuclease activity of preparations of human lymphoblastoid interferon.

Crude human lymphoblastoid interferon has less ribonuclease activity than equivalent primary leukocyte interferon and ribonuclease was eliminated when it was purified. The methods used differed from those that had failed to eliminate similar activity from leukocyte interferon. This result makes it unlikely that exogenous ribonuclease plays a major role in the antiviral action of interferon preparations.

Burkitt Lymphoma↗
PubMed1977

Influence of renal insufficiency on levels of serum ribonuclease in patients with multiple myeloma.

Serum RNase levels were measured in 34 patients with multiple myeloma and compared with 51 normal controls and 28 non-myeloma patients on chronic hemodialysis. Nineteen of the myeloma patinets with creatinine clearance (CCr) greater than 50 ml/minute had mean serum RNase levels that were statistically indistinguishable from those of the normal controls. The 15 myeloma patinets with CCr less than 50 ml/minute had mean RNase levels much higher than normal controls or myeloma patients with normal renal function. Patients without myeloma but on hemodialysis for chronic renal failure of varied etiologies had markedly elevated serum RNase levels. A strong correlation between RNase levels and renal insufficiency, as measured by CCr, has thus been demonstrated. In addition, case histories of 5 representative myeloma patients were analyzed in greater detail; they illustrated the rise and fall of RNase levels as a function of the status of their renal insufficiency, regardless of the extent of the underlying myeloma. We concluded that the serum RNase level was an indicator of renal function, and was not a biomarker either for the presence or extent of the plasma cell tumor.

Creatinine↗
PubMed1977

RNase activity in human interferon preparations.

The level of RNase activity in human interferon preparations was examined. Although sequential purification of interferon resulted in nearly a 300-fold increase in specific activity, RNase-specific activity remained more or less constant. The implications of this finding for the analyses of the mode of action of interferon are discussed.

Humans↗