Purification and immunochemical analysis of cytochrome c from Neurospora crassa

Susan Stade, Robert Brambl

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Abstract

Procedures were refined and improved for the purification of cytochrome c from Neurospora crassa, for development of specific antisera to the protein, and for immunochemical identification of cytochrome c after in vivo synthesis and radiolabeling with 3H and 35Fe. The cytochrome c was obtained in high yields via column chromatography and salt fractionation, and the product was pure as judged by spectrophotometric and electrophoretic criteria. Effective, specific antisera to cytochrome c could be obtained only after the monomeric protein antigen was crosslinked with glutaraldehyde; immunoprecipitation of cytochrome c synthesized in vivo was achieved efficiently with a double-antibody procedure.

Original languageEnglish (US)
Pages (from-to)186-190
Number of pages5
JournalExperimental Mycology
Volume4
Issue number2
DOIs
StatePublished - Jun 1980

Bibliographical note

Funding Information:
This research was supported by NIH Research Grant GM-19398 from the National Institute of General Medical Sciences.

Keywords

  • Neurospora crassa
  • cytochrome c, immunochemical identification, purification
  • double-antibody procedure

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