The regulation of protein synthesis in nephrotic rat kidney ribosome preparations

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Abstract
The incorporation of 14C-leucine and 14C-phenylalanine into protein was measured in ribosomes following the deoxycholate treatment of microsomes from control and nephrotic rat kidney homogenates. The pH 5 enzyme fraction was obtained from postmicrosomal supernatant (S105) of control and nephrotic kidney homogenates. The incorporation was markedly increased in the nephrotic preparations and depended on changes in both the ribosomes and pH 5 enzymes. The increase was present in the presence of either endogenous mRNA or synthetic mRNA (poly U). It was associated with increased binding of aminoacyl-tRNA as well as increased incorporation of aminoacyl-tRNA into peptide. Active ribonuclease activity was decreased in nephrotic kidney S105, pH 5 enzymes, and microsomes compared to comparable fractions in control kidney. Total ribonuclease activity was also decreased in nephrotic kidney in these fractions. No increase in polysome content was found in these ribosomes prepared with deoxycholate but when deoxycholate was eliminated, a crude homogenate of nephrotic kidney had twice as many polysomes.

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