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Purification and mode of action of exoribonuclease from bovine brain.

作者信息

Guha A

出版信息

J Biol Chem. 1977 Sep 25;252(18):6416-20.

PMID:893414
Abstract

The exoribonuclease in bovine brain has been purified about 900-fold in 10% yield. The molecular weight is about 65,000. The enzyme is free from other ribonucleases of bovine brain. Studies of the mode of action of the enzyme show the following: (a) The enzyme cleaves both oligo- and polyribonucleotides exonucleolytically, initiating nucleolytic attack from the 5'-hydroxyl end to yield 3'-mononucleotides. The enzyme differs from spleen exonuclease in that it does not act on polydeoxyribonucleotides. (b) When the 5'-hydroxyl group is phosphorylated, the enzyme is inactive. (c) The enzymic action is processive in nature; the enzyme hydrolyzes one polynucleotide chain to completion before proceeding to the degradation of another chain.

摘要

相似文献

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引用本文的文献

1
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