| Literature DB >> 795666 |
P Zimniak, E Hartter, W Woloszczuk, H Ruis.
Abstract
Catalase A from Saccharomyces cerevisiae and its biosynthetic precursors can specifically be immunoprecipitated from extracts obtained from yeast cells grown in the presence of L-[3H]leucine or 59FeCl3. The enzyme and its precursors recognized by a specific antiserum are absent from anaerobic cells. During oxygen adaptation of yeast pre-grown on 0.3% glucose under anaerobic conditions catalase A is formed via a heme-less precursor, probably the apomonomer of the protein, and a heme-containing intermediate. When cells are grown in the presence of Tween 80 the amount of catalase A, but not of catalase T, increases 4-fold. Comparison of the mode of synthesis of catalase T and A shows that no precursor-product relationship exists between the two proteins.Entities:
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Year: 1976 PMID: 795666 DOI: 10.1111/j.1432-1033.1976.tb11126.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956