Title : The effect of tetrahydrobiopterin on the in situ phosphorylation of tyrosine hydroxylase in rat striatal synaptosomes.

Pub. Date : 1994 May

PMID : 7915013






5 Functional Relationships(s)
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1 Tetrahydrobiopterin (BH4), the obligatory cofactor of the aromatic amino acid hydroxylases, decreased the in situ 32P-phosphorylation of tyrosine hydroxylase (TH) in rat striatal synaptosomes. Phosphorus-32 tyrosine hydroxylase Rattus norvegicus
2 Tetrahydrobiopterin (BH4), the obligatory cofactor of the aromatic amino acid hydroxylases, decreased the in situ 32P-phosphorylation of tyrosine hydroxylase (TH) in rat striatal synaptosomes. Phosphorus-32 tyrosine hydroxylase Rattus norvegicus
3 Incubation of pre-32P-labeled synaptosomes with BH4 in the presence of a permeant analogue of cAMP decreased the cAMP-stimulated level of 32P label incorporation into TH by about 50%, as determined by immunoprecipitation and autoradiography of SDS-polyacrylamide gels. Phosphorus-32 tyrosine hydroxylase Rattus norvegicus
4 Incubation of pre-32P-labeled synaptosomes with BH4 in the presence of a permeant analogue of cAMP decreased the cAMP-stimulated level of 32P label incorporation into TH by about 50%, as determined by immunoprecipitation and autoradiography of SDS-polyacrylamide gels. Phosphorus-32 tyrosine hydroxylase Rattus norvegicus
5 A similar decrease in the amount of TH 32P-labeling was observed with the precursor of BH4, sepiapterin. Phosphorus-32 tyrosine hydroxylase Rattus norvegicus