Plant Nucleases. II. Properties of Corn Ribonucleases I and II and Corn Nuclease I
Author(s) -
Curtis M. Wilson
Publication year - 1968
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.43.9.1339
Subject(s) - ribonuclease , nuclease , nucleotide , purine , biochemistry , ribonuclease iii , rna , rnase p , ribonuclease t1 , endonuclease , chemistry , dna , enzyme , biology , gene , rna interference
A classification system is presented to distinguish 3 corn nucleases-Ribonuclease I, Ribonuclease II, and Nuclease I-which were described in the first paper of this series. The 2 ribonucleases are specific for RNA, are endonucleases, and liberate purine and pyrimidine cyclic nucleotides from dinucleotide monophosphates as well as from RNA. Ribonuclease I and II hydrolyze the purine cyclic nucleotides to 3'-nucleotides, while Ribonuclease II may also act on the pyrimidine cyclic nucleotides. Ribonuclease II is best characterized by its molecular weight of 17,000, by a higher pH optimum than Ribonuclease I, and by its absorption onto microsomes.Nuclease I is a partially purified endonuclease which produces 5'-nucleotides from RNA, DNA, and dinucleotide monophosphates. The same enzyme may also be a 3'-nucleotidase.The corn nucleases were compared with nucleases found in other plant species.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom