Purification and properties of a ribonuclease from corn leaf tissues |
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| Institution: | 1. Department of Cellular Biochemistry, University Medical Center Goettingen, Humboldtallee 23, D-37073 Goettingen, Germany;2. Research Group Structure and Function of Molecular Machines, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, D-37077 Goettingen, Germany;3. Cluster of Excellence Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells (MBExC), University of Goettingen, D-37075 Goettingen, Germany |
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| Abstract: | An acid endoribonuclease isolated from corn leaf tissues was purified 530 times. Gel electrophoresis indicated that the enzyme was homogeneous. The enzyme showed an optimum pH at 5.5 and an apparent molecular weight of 32 000. Corn RNase attacks natural RNAs and synthetic polyribonucleotides and the relative rate of degradation was poly U > yeast RNA > E. coli tRNA > poly A ⪢ poly C. Zn2+, Mg2+, Mn2+ and EDTA inhibited the enzyme activity. No stimulation by K+ was observed. Cu2+ and heparin had no effect on the activity. The results suggest that the investigated RNase differs from other known corn ribonucleases. |
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