Preliminary purification and characterization studies of a low molecular weight, high affinity cytosolic lead-binding protein in rat brain |
| |
Authors: | G DuVal B A Fowler |
| |
Affiliation: | Department of Pathology, University of Maryland School of Medicine, Baltimore 21201. |
| |
Abstract: | Carrier-free 203Pb has been used to label high affinity lead-binding proteins in rat brain cytosol to allow their initial characterization. The low molecular weight 203Pb-protein complex collected from a Sephadex G-75 column eluate has been further purified by Sephadex DEAE chromatography and then partially characterized. The protein has a molecular weight of 23,000 daltons as determined by SDS polyacrylamide gel electrophoresis and significant levels of glutamic acid (9.3%), aspartic acid (10.8%) and cysteine (9.4%). Western blot studies conducted using the polyclonal antibody to the renal lead-binding proteins showed a lack of reactivity, indicating that the brain protein is immunologically distinct from that found in the kidney. |
| |
Keywords: | |
|
|