Open AccessSpecific Inactivation of Fructose 1,6‐Bisphosphatase from Saccharomyces cerevisiae by a Yeast Protease
Author(s) -
Molano Jesús,
Gancedo Carlos
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03475.x
Subject(s) - yeast , biochemistry , malate dehydrogenase , fructose 1,6 bisphosphatase , fructose , glutamate dehydrogenase , ammonium sulfate , saccharomyces cerevisiae , dehydrogenase , protease , enzyme , rhodotorula , isomerase , chemistry , biology , chromatography , glutamate receptor , receptor
A fraction has been isolated from baker's yeast that is able to inactivate fructose 1,6‐bisphos‐phatase in vitro . The inactivating fraction is heat labile, non‐dialysable and is precipitated with ammonium sulfate; thus indicating that it is a protein. Malate dehydrogenase, hexokinase, glucose phosphate isomerase, glucose‐6‐phosphate dehydrogenase, glutamate dehydrogenase and catalase from baker's yeast and fructose 1,6‐bisphosphatase from the yeast Rhodotorula glutinis were not inactivated by the preparation. A fraction which is able to inhibit the inactivating factor has also been found in baker's yeast. The inhibitor is thermoresistant, non‐dialysable and precipitable by ammonium sulfate. The possible biological significance of these findings in relation with the regulation of yeast fructose 1,6‐bisphosphatase is considered.