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M A Siwecka

Publications and source records attributed to M A Siwecka.

5 recordsLinked to original sources

Purification and characterization of nuclease I associated with rye germ ribosomes.

A nuclease has been purified about 100-fold from ammonium chloride wash of rye germ ribosomes. The enzyme was electrophoretically homogeneous. Its M, was 20,000 and pl 4.8. The neclease hydrolyzed endonuclelytically DNA and RNA and was accompanied by 3-nucleotidase activity. The enzyme degraded RNA to oligonucleotides with a phosphomonoester bond at position 5', and both denatured and native DNA to 5'-OH and 3'-phosphate-terminated fragments. Zinc ions and 2-mercaptoethanol stimulated deoxyribonucleolytic activity. EDTA, polyamines and heparin had only little or no effect. The enzyme is a glycoprotein containing 28% of carbohydrate which consists of fucose, mannose and glucosamine. The nuclease isolated is classified as nuclease I.

Carbohydrates

The presence of deoxyribonucleolytic activity in cytoplasmic ribosomes of rye (Secale cereale L) germs.

Deoxyribonucleolytic activity was found to be associated with cytoplasmic ribosomes and ribosomal subunits of rye germs. The activity has the pH optimum at 5.0. Treatment of ribosomes and 60S subunits with 0.5 M-ammonium chloride released a considerable part of deoxyribonucleolytic and ribonucleolytic activity; treatment of 40S subunits resulted in a complete release of deoxyribonucleolytic activity and partial release of ribonucleolytic activity. This suggests the presence in ribosomes of rye germs of two types of nucleolytic enzymes: an enzyme of the nuclease I type with deoxyribonuclease and ribonuclease activities, and typical ribonucleases hydrolysing RNA only.

Ammonium Chloride