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Purification of a Corn Ribonuclease

From the ¹ From the Crops Research Division, Agricultural Research Service, United States Department of Agriculture, and Department of Agronomy, University of Illinois, Urbana, Illinois 61801

A ribonuclease was purified 4,100 times from corn seed meal. The enzyme was homogeneous on analytical gel filtration and has an estimated molecular weight of 23,000 from the gel filtration data. The RNase from Illinois Low Protein corn gave two bands on disc electrophoresis, while the RNase from two hybrids gave only a single band. The amino acid composition of the RNases from the two sources was essentially the same. The RNase liberates cyclic nucleotides from dinucleotides, and is more active on the purine residues. Only purine cyclic nucleotides are hydrolyzed at an appreciable rate.

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