Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase Journal Article


Authors: Evers, M. E.; Huhse, B.; Titorenko, V. I.; Kunau, W. H.; Hartl, F. U.; Harder, W.; Veenhuis, M.
Article Title: Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase
Abstract: We used peroxisomal alcohol oxidase (AO) for the affinity purification Of molecular chaperones from yeasts. Methodical studies showed that up to 0.8 mg of purified bacterial GroEL was able to bind per ml of immobilized denatured AO column material. Using crude extracts of Hansenula polymorpha or Saccharomyces cerevisiae, several proteins were specifically eluted with Mg-ATP which were recognized by antibodies against hsp60 or hsp70. One H. polymorpha 70 kDa protein was strongly induced during growth at elevated temperatures, whereas a second 70 kDa protein as well as a 60 kDa protein showed strong protein sequence homology to mitochondrial SSC1 and hsp60, respectively, from S. cerevisiae.
Keywords: proteins; complex formation; chaperone; saccharomyces-cerevisiae; alcohol oxidase; peroxisome; hsp; hansenula-polymorpha
Journal Title: FEBS Letters
Volume: 321
Issue: 1
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1993-04-01
Start Page: 32
End Page: 36
Language: English
ACCESSION: WOS:A1993KX62100008
DOI: 10.1016/0014-5793(93)80615-2
PROVIDER: wos
PUBMED: 8096822
Notes: Article -- Source: Wos
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  1. F. Ulrich Hartl
    75 Hartl