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Adv Exp Med Biol. 1998;442:441-7.

Increased phosphorylation of specific rat cardiac and retinal proteins in taurine-depleted animals: isolation and identification of the phosphoproteins.

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  • 1Department of Pharmacology, Texas Tech University Health Sciences Center, Lubbock 79430, USA.


Partial depletion of the tissue levels of taurine in the alive animal stimulates in vitro phosphorylation of both an approximately 20 kDa (94%) and an approximately 44 kDa (85%) protein present in subcellular fractions of the rat retina and heart. Tissue levels of taurine were reduced by feeding the animals 1.5% guanidinoethanesulfonic acid (GES) in their drinking water for 6 weeks. The increase in the in vitro phosphorylation of both the approximately 20 kDa and approximately 44 kDa proteins was reversed when the animals were subsequently given 1.5% taurine in their drinking water for an additional 6 weeks. Isolation, purification, tryptic digestion, and peptide sequence analysis of the retinal approximately 20 kDa phosphoprotein suggest that it is histone H2B. However, the results are ambiguous due to an impurity (< 25%) in the retinal preparation. Sequence analysis of the approximately 44 kDa phosphoprotein indicates that it is pyruvate dehydrogenase.

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