Purification of thiamine-binding protein of rat erythrocytes by affinity chromatography

Voskoboev, A I; Averin, V. A.

doi:10.1007/bf00837578

Cited by 1 publication

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“…In particular, it would be worthwhile to gain a better insight into the mitochondrial metabolism of TPP, which represents 30% of the total cellular cofactor in hepatocytes [4]. As far as TPP synthesis and localisation are concerned, the possibility of TPP synthesis in RLM has long since been ruled out [5, 6]. Consistently, in hepatocytes, externally added thiamine is converted to TPP via the cytosolic thiamine pyrophosphokinase (EC 2.7.6.2) [7], with TPP being taken up by RLM in a carrier‐mediated process [8].…”

Section: Introductionmentioning

confidence: 99%

Rat liver mitochondria can hydrolyse thiamine pyrophosphate to thiamine monophosphate which can cross the mitochondrial membrane in a carrier‐mediated process

et al. 1998

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We show here that TPPCTMP conversion can take place in rat liver mitochondria. This occurs via the novel, putative TPP pyrophosphatase localised in the mitochondrial matrix, as shown both by digitonin titration and by an HPLC enzyme assay carried out on the mitochondrial matrix fraction. Certain features of the reaction, including the substrate and pH dependence, are reported. Additional evidence is given that externally added TMP can cross the mitochondrial membrane in a manner consistent with the occurrence of a carrier-mediated process. This can occur both via the TPP translocator and via a novel translocator, inhibited by CAT but different from the ADP/ATP carrier.z 1998 Federation of European Biochemical Societies.

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