Formation of a complex between yeast proteinases A and B.
Sephadex G-100 gel filtration of a purified mixture of tryptophan-synthase-inactivating enzymes I and II from Saccharomyces cerevisiae, which had previously been identified as yeast proteinases A and B, yields two coincident peaks of tryptophan-synthase- inactivating activity and proteinase A and B activities. The peaks correspond to molecular weights of approximately 100 000 and 50 000. It could be demonstrated, with purified proteinases A and B, that the high molecular weight peaks is due to the formation of a stoichiometric complex between proteinases A and B. The AB complex can easily be separated into its constituent enzymes by DEAE-Sephadex chromatography. When in the AB complex, proteinase B molecules still bind the specific proteinase B inhibitor from yeast.[1]References
- Formation of a complex between yeast proteinases A and B. Hinze, H., Betz, H., Saheki, T., Holzer, H. Hoppe-Seyler's Z. Physiol. Chem. (1975) [Pubmed]
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