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Updated: Aug 8, 2026

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Isolation and some properties of bovine brain 100 kDa heat shock protein
H Itoh1, R Kobayashi, Y Tashima
1Department of Biochemistry, Akita University School of Medicine, Japan.
Abstract:
1. The 100 kDa protein was purified from bovine brains. 2. The antibody against the 100 kDa brain protein was prepared and was monospecific to the antigen. 3. The antibody cross-reacted with HeLa cell HSP100 (100 kDa heat shock protein). 4. The physicochemical, immunochemical properties and a partially amino acid sequence indicated that the 100 kDa protein was HSP100. 5. Peptide mapping using Staphylococcus aureus V8 protease showed a core peptide with 10 kDa molecular mass common to both HSP100 and HSP90. 6. The amino acid sequence of the 10 kDa fragment of the 100 kDa protein showed a high homology with that of human HSP90 (38-60); the difference was only two of 23 amino acid residues determined.
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