The activity of pyruvate carrier in a reconstituted system: Substrate specificity and inhibitor sensitivity Export

@article{citeulike:764232, abstract = {The pyruvate carrier, of molecular mass 34 kDa, was purified from mitochondria isolated from rat liver, rat brain, and bovine heart, by affinity chromatography on immobilized 2-cyano-4-hydroxycinnamate. Its activity after reconstitution in phosphatidylcholine vesicles was measured either as uptake of [1-14C]pyruvate or as exchange with different 2-oxoacids. All preparations exhibited similar apparent Km values for pyruvate, but somewhat different Vmax values. The ability to exchange different anions of physiological significance, including branched-chain 2-oxoacids, confirmed the known substrate specificity described for the pyruvate carrier in mitochondria. The sensitivity of pyruvate transport toward phenylglyoxal suggested an important role of arginyl residues in the transport activity, while a role of lysyl and histydyl residues was not confirmed.}, author = {Nalecz, Katarzyna A. and Kaminska, Joanna and Nalecz, Maciej J. and Azzi, Angelo}, citeulike-article-id = {764232}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/0003-9861(92)90655-G}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WB5-4DPC4KR-1PP/2/2d7f3bef69f635ba1e54ca5c8826188d}, day = {15}, doi = {10.1016/0003-9861(92)90655-G}, journal = {Archives of Biochemistry and Biophysics}, keywords = {14c, pyruvate-transport}, month = {August}, number = {1}, pages = {162--168}, posted-at = {2006-07-19 11:06:13}, priority = {2}, title = {The activity of pyruvate carrier in a reconstituted system: Substrate specificity and inhibitor sensitivity}, url = {http://dx.doi.org/10.1016/0003-9861(92)90655-G}, volume = {297}, year = {1992} }

TY - JOUR ID - citeulike:764232 L3 - citeulike-article-id:764232 N2 - The pyruvate carrier, of molecular mass 34 kDa, was purified from mitochondria isolated from rat liver, rat brain, and bovine heart, by affinity chromatography on immobilized 2-cyano-4-hydroxycinnamate. Its activity after reconstitution in phosphatidylcholine vesicles was measured either as uptake of [1-14C]pyruvate or as exchange with different 2-oxoacids. All preparations exhibited similar apparent Km values for pyruvate, but somewhat different Vmax values. The ability to exchange different anions of physiological significance, including branched-chain 2-oxoacids, confirmed the known substrate specificity described for the pyruvate carrier in mitochondria. The sensitivity of pyruvate transport toward phenylglyoxal suggested an important role of arginyl residues in the transport activity, while a role of lysyl and histydyl residues was not confirmed. IS - 1 JF - Archives of Biochemistry and Biophysics EP - 168 TI - The activity of pyruvate carrier in a reconstituted system: Substrate specificity and inhibitor sensitivity VL - 297 SP - 162 KW - 14c KW - pyruvate-transport AU - Nalecz, Katarzyna AU - Kaminska, Joanna AU - Nalecz, Maciej AU - Azzi, Angelo PY - 1992/08/15/ UR - http://dx.doi.org/10.1016/0003-9861(92)90655-G ER -