Inhibition of bovine and human brain 2′:3′-cyclic nucleotide 3′-phosphodiesterase by heparin and polyribonucleotides and evidence for an associated 5′-polynucleotide kinase activity

Terry Joe Sprinkle, Russell B. Tippins, Daniel Kestler

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The present paper establishes a 5′-polynucleotide kinase activity associated with the bovine and human brain enzyme 2′:3′-cyclic nucleotide 3′-phosphodiesterase (EC 3.1.4.37) in addition to known extremely high hydrolysis rates against 2′:3′-cyclic nucleotides. Modulation of the enzyme activity by the addition of polyadenylate (5′) and polyuridylate (5′), histone F3, myelin basic protein (MBP), and other basic molecules suggest that RNA may be the natural substrate for both enzymes. These enzymes, isolated from brain and present in very high activities in oligodendrocytes and in isolated myelin, probably have complex functions.

Original languageEnglish (US)
Pages (from-to)686-691
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume145
Issue number2
DOIs
StatePublished - Jun 15 1987
Externally publishedYes

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Polyribonucleotides
Polynucleotide 5'-Hydroxyl-Kinase
Cyclic Nucleotides
Phosphoric Diester Hydrolases
Heparin
Brain
Enzymes
Myelin Basic Protein
Enzyme activity
Histones
Hydrolysis
Oligodendroglia
Myelin Sheath
Modulation
RNA
Molecules
Substrates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "The present paper establishes a 5′-polynucleotide kinase activity associated with the bovine and human brain enzyme 2′:3′-cyclic nucleotide 3′-phosphodiesterase (EC 3.1.4.37) in addition to known extremely high hydrolysis rates against 2′:3′-cyclic nucleotides. Modulation of the enzyme activity by the addition of polyadenylate (5′) and polyuridylate (5′), histone F3, myelin basic protein (MBP), and other basic molecules suggest that RNA may be the natural substrate for both enzymes. These enzymes, isolated from brain and present in very high activities in oligodendrocytes and in isolated myelin, probably have complex functions.",
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T1 - Inhibition of bovine and human brain 2′:3′-cyclic nucleotide 3′-phosphodiesterase by heparin and polyribonucleotides and evidence for an associated 5′-polynucleotide kinase activity

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AU - Tippins, Russell B.

AU - Kestler, Daniel

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N2 - The present paper establishes a 5′-polynucleotide kinase activity associated with the bovine and human brain enzyme 2′:3′-cyclic nucleotide 3′-phosphodiesterase (EC 3.1.4.37) in addition to known extremely high hydrolysis rates against 2′:3′-cyclic nucleotides. Modulation of the enzyme activity by the addition of polyadenylate (5′) and polyuridylate (5′), histone F3, myelin basic protein (MBP), and other basic molecules suggest that RNA may be the natural substrate for both enzymes. These enzymes, isolated from brain and present in very high activities in oligodendrocytes and in isolated myelin, probably have complex functions.

AB - The present paper establishes a 5′-polynucleotide kinase activity associated with the bovine and human brain enzyme 2′:3′-cyclic nucleotide 3′-phosphodiesterase (EC 3.1.4.37) in addition to known extremely high hydrolysis rates against 2′:3′-cyclic nucleotides. Modulation of the enzyme activity by the addition of polyadenylate (5′) and polyuridylate (5′), histone F3, myelin basic protein (MBP), and other basic molecules suggest that RNA may be the natural substrate for both enzymes. These enzymes, isolated from brain and present in very high activities in oligodendrocytes and in isolated myelin, probably have complex functions.

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