PMID: 8613944Apr 1, 1996Paper

Determination and metabolism of dithiol chelating agents. XVII. In humans, sodium 2,3-dimercapto-1-propanesulfonate is bound to plasma albumin via mixed disulfide formation and is found in the urine as cyclic polymeric disulfides

The Journal of Pharmacology and Experimental Therapeutics
R M MaiorinoH V Aposhian

Abstract

The binding of 2,3-dimercapto-1-propanesulfonate (DMPS) in plasma was determined in three healthy young adults after a single 300-mg p.o. dose. By 5 hr after DMPS administration, 62.5% of the total plasma DMPS was bound to proteins. The remainder consisted of nonprotein associated DMPS disulfides (36.6%) and unaltered DMPS (0.9%). Protein-bound DMPS consisted of a DMPS-albumin complex (84%) and a higher molecular weight protein complex (16%), perhaps albumin aggregates. DMPS was released from the isolated DMPS-albumin complex after treatment with dithiothreitol, indicating that it was bound via a disulfide linkage. The half-life of unaltered DMPS was 1.8 hr, whereas that of altered DMPS was 20 hr, suggesting that the DMPS-albumin disulfide complex is stable and that DMPS was released from it slowly. In addition, the biotransformation of OMPS to disulfide forms was extensive. By 9 hr after administration, 10% of the total urinary DMPS was unchanged drug and 90% was altered DMPS. The latter was converted to DMPS by dithiothreitol, indicating that the altered DMPS consisted of disulfides. In 2- to 4-hr urine, DMPS disulfides included cyclic polymeric DMPS disulfides (97%), DMPS-cysteine (1:2) mixed disulfide (2.5%) and acyclic DMP...Continue Reading

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