The development in primary dissociated rat brain cultures of 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) activity, the accumulation of CNP protein, and the number of cells accumulating this protein have been quantitatively determined as a function of time in culture. Parallel determinations ha
Molecular cloning and characterization of rat brain 2′, 3′ -cyclic nucleotide 3′ -phosphodiesterase isoform 2
✍ Scribed by M. Gravel; D. DeAngelis; P. E. Braun
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 566 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
We have isolated a cDNA coding for the larger isoform of the rat brain 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP2), a protein associated with myelination in the central nervous system (CNS). The complete 420 amino acid sequence was deduced from the nucleotide sequence of the cDNA. Sequence comparisons show that rat CNP shares 96% homology with mouse, 84% with bovine, and 86% with human CNP. Errors in the published sequence of rat CNPl have now been corrected. Comparisons with other proteins reveal several interesting conserved motifs, including two leucine repeat heptads, and two consensus motifs for phosphorylation in the N-terminal domain of CNPZ.
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