Volume 9 Issue 2, June 1999: 135-144
ORIGINAL ARTICLES
Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells
XU Cun Shuan1,*, Wei Ming ZHANG1, Dieter TECHEL 2, Marco MEYER2, Yan Zhang LI1, Ludger RENSING2,*
1. Department of Biology, Henan Normal University, Xinxiang 453002, China
2. Institute of Cell Biology, Bremen University, D-28359 Bremen, Germany
Correspondence:
The 45, 55, 65 and 100 kDa ATP-binding proteinases (ATP-BPases) of the heat-shocked (44 ℃ for 30 min, recovery for 12 h) rat C6 glioma cells were purified by DEAE-ionexchange and ATP-affinity chromatography. Their molecular masses, isoelectric points (pI), pH-optima and other properties were analyzed by native proteinase gels. It was shown that the 65 kDa ATP-BPase is specifically induced by heat shock and not detectable in control cells. Its N-terminal 1-9 amino acid sequence was determined by Edman degradation, but no homologies to other proteins in the protein data bases were found. 30 and 31 kDa proteinases can be cleaved from the 45, 55 and 65 kDa proteinases to which they are linked. A possible relationship of the heat-induced 65 kDa ATP-BPase with the ATP-dependent proteinases (ATP-DPases) in prokaryotes and eukaryotes is discussed.
FULL TEXT | PDF
Browse 1967
