Late-infantile Batten disease: Purification of the subunit c of the mitochondrial ATP synthase from storage material

Kevork Hagopian, B. D. Lake, B. G. Winchester, J. B. Clark

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The accumulation of subunit c of the mitochondrial ATP synthase in late- infantile neuronal lipofuscinosis (LINCL) and juvenile neuronal lipofuscinosis (JNCL) is well documented. The purification of the subunit from diverse sources has been reported previously, although not from the brain of Batten disease patients. This proteolipid has now been purified from late-infantile Batten disease brain. The procedures used were an original combination of the conventional solubilisation, differential centrifugation, organic solvent extractions, preparative gel electrophoresis, and FPLC. Gel filtration of the purified protein indicated molecular mass equal to or greater than 2 x 106 Da; however, electrophoresis of this pure protein suggested a molecular mass of approximately 3,500 Da, which is a characteristic of subunit c. The pure protein may be solubilised in aqueous buffer containing <1% lithium dodecyl sulphate (LDS). The protein binds dicyclohexylcarbodiimide (DCCD) and shows immunoreactivity to antibodies raised against ovine storage bodies.

Original languageEnglish (US)
Pages (from-to)272-278
Number of pages7
JournalAmerican Journal of Medical Genetics
Volume57
Issue number2
DOIs
StatePublished - Jun 16 1995
Externally publishedYes

Keywords

  • DCCD
  • late-infantile Batten disease
  • lysosomal storage
  • mitochondrial ATP synthase
  • proteolipid
  • subunit c purification

ASJC Scopus subject areas

  • Genetics(clinical)

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