Fluorometric detection of low temperature thermal transitions in the Clq component of human complement

Paul M. Horowitz, Zymunt Wasylewski, William P. Kolb

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Fluorescence studies with the human complement component Clq were performed as a function of temperature and demonstrated the existence of low temperature, thermally induced structural transitions in the Clq molecule. Both intrinsic protein fluorescence and the fluorescence of the apolar probe 2-p-toluidinylnaphthalene-6-sulfonate independently showed thermal transitions at 15°C, 35°C and 48°C. Clq activity measurements indicated no loss of hemolytic activity at temperatures below 46°C. It is proposed that these structural transitions are a consequence of the internal flexibility of the native Clq molecule.

Original languageEnglish (US)
Pages (from-to)382-387
Number of pages6
JournalTopics in Catalysis
Volume96
Issue number1
DOIs
StatePublished - 1980
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

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