More Effective Mobilization of Hg²⁺ from Human Serum Albumin Compared to Cd²⁺ by L-Cysteine at Near-Physiological Conditions.

ABSTRACT: Although chronic low-level exposure to Hg²⁺ and Cd²⁺ causes human nephrotoxicity, the bioinorganic processes that deliver them to their target organs are poorly understood. Since the plasma protein human serum albumin (HSA) has distinct binding sites for these metal ions, we wanted to gain insight into these translocation processes and have employed size-exclusion chromatography coupled on-line to an inductively coupled plasma atomic emission spectrometer using phosphate-buffered saline mobile phases. When HSA 'labeled' with Hg²⁺ and Cd²⁺ (1:0.1:0.1) using 300 μM of L-methionine was analyzed, the co-elution of a single C, S, Cd, and Hg peak was observed, which implied the intact bis-metalated HSA complex. Since human plasma contains small molecul

SUBMITTER: Gautam A 

PROVIDER: S-EPMC10383730 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature