Abstract
A plant endonuclease with 3'-nucleotidase activity was purified from scallion bulbs to homogeneity as judged by SDS-PAGE. The molecular weight of the enzyme was estimated to be 38, 000 by SDS-PAGE and 40, 000 by Sephadex G-100 gel filtration. The enzyme rapidly hydrolyzed yeast RNA and denatured calf thymus DNA to acid-soluble substances, and hydrolyzed the plasmid pBR322 to yield small DNA fragments at low enzyme concentrations. These four activities were eliminated by treatments with EDTA and tetraethylenepentamine. The enzyme had maximum activity at pH 8.5-9.0 for 3'-AMP, 3'-GMP, and 3'-UMP, at pH 6.5 for 3'-CMP and yeast RNA, and at pH 6.0 for denatured calf thymus DNA and pBR322. During digestion of yeast RNA by the enzyme at pH 6.5, 5'-GMP was released most rapidly, followed by 5'-UMP, 5'-AMP, and 5'-CMP. These properties were different from those of endonucleases isolated from other sources such as mung bean sprouts and wheat seedlings.
