Further studies on thermal denaturation of pyruvate dehydrogenase complex from bacillus stearothermophilus

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita, Yoshikatsu Aikawa, Masatsune Ishiguro

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Thermally induced changes in pyruvate dehydrogenase complex (PDC) from B. stearothermophilus were examined mainly at temperatures from 60° to 70°C. Accompanied by inactivation of pyruvate decarboxylase, light scattering decreased, and ANS fluorescence increased. These changes including the inactivation were approximately first-order reactions, and the values of rate constants were greatly dependent on temperature. Chromatographic studies showed that any polypeptides were in associated forms and that final products were aggregates (> 230S) and an assembly (48S) smaller than PDC. The aggregates and assembly were rich in decarboxylase and lipoate acetyltransferase, respectively. It was suggested that, during the thermal denaturation, a decarboxylase was dissociated from PDC and immediately involved in aggregates.

Original languageEnglish
Pages (from-to)1126-1132
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume61
Issue number7
DOIs
Publication statusPublished - Jan 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Further studies on thermal denaturation of pyruvate dehydrogenase complex from bacillus stearothermophilus'. Together they form a unique fingerprint.

  • Cite this