The binding of silica to proteins from plasma and lungs of rat: In vitro

Shivendra V. Singh, Ballabh Das, M. Firoze Khan, Qamar Rahman, P. N. Viswanathan

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Silica dissolving out from the slate dust was found to bind with plasma protein and purified bovine serum albumin. At 24 h of incubation at 37°C binding affinity of silica (μg of silica bound/mg of protein) with plasma protein and bovine serum albumin was found to be 0.59 and 0.44, respectively. By molecular exclusion chromatography using Sephadex G-200, silica binding protein of plasma was determined to be of mol. wt. around 67 000. Similar proteins having silica binding capacity (mol. wt. 70 000 and 85 000) were also found in rat lung but these proteins unlike their plasma counterpart were glycoprotein in nature. Polyacrylamide gel electrophoresis of plasma and protein rich lung fraction show that proteins upon binding with silica undergo mobility changes. Significance of the existence of silica binding protein in plasma and lung of rat in relation to silica toxicity is discussed.

Original languageEnglish (US)
Pages (from-to)155-164
Number of pages10
JournalChemico-Biological Interactions
Issue number1-2
StatePublished - Apr 1984
Externally publishedYes


  • Binding protein
  • Interaction
  • Silicates
  • Slate dust

ASJC Scopus subject areas

  • Toxicology


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