Specific inactivation of fructose 1,6-bisphosphatase from Saccharomyces cerevisiae by a yeast protease.
Specific inactivation of fructose 1,6-bisphosphatase from Saccharomyces cerevisiae by a yeast protease.
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酵母蛋白酶对酿酒酵母果糖 1,6-双磷酸酶进行特异性灭活。
DOI：
10.1111/j.1432-1033.1974.tb03475.x
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
C. Gancedo
中科院分区：
文献类型：
--
作者：
J. Molano;C. Gancedo
从面包酵母中分离出一种能在体外降解果糖1，6-二磷酸酶的组分。灭活部分对热不稳定，不可透析，用硫酸铵沉淀;因此表明其为蛋白质。来自面包酵母的苹果酸脱氢酶、己糖激酶、葡萄糖磷酸异构酶、葡萄糖-6-磷酸脱氢酶、谷氨酸脱氢酶和过氧化氢酶以及来自酵母红酵母的果糖1，6-二磷酸酶未被该制剂灭活。
在面包酵母中也发现了一种能够抑制失活因子的组分。该缓蚀剂具有耐温、不可透析、可被硫酸铵沉淀等特点。这些研究结果与酵母果糖1，6-二磷酸酶的调节可能的生物学意义被认为是。
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.