Neeff J, Hägele E, Nauhaus J, Heer U, Mecke D
Eur J Biochem. 1978 Jul 3;87(3):489-95. doi: 10.1111/j.1432-1033.1978.tb12399.x.
The cytoplasmic malate dehydrogenase of Saccharomyces cerevisiae was radioactively labeled during its synthesis on a glucose-free derepression medium. After purification a sensitive radio-immunoassay for this enzyme could be developed. The assay showed that after the physiological, glucose-dependent 'catabolite inactivation' of cytoplasmic malate dehydrogenase an inactive enzyme protein is immunologically not detectable. Together with the irreversibility of this reaction in vivo this finding strongly suggest a proteolytic mechanism of enzyme inactivation. For this process the term 'catabolite degradation' is used.
酿酒酵母的细胞质苹果酸脱氢酶在无糖去阻遏培养基上合成过程中被放射性标记。纯化后,可开发出针对该酶的灵敏放射免疫测定法。该测定法表明,在细胞质苹果酸脱氢酶发生生理性的、依赖葡萄糖的“分解代谢物失活”后,无法通过免疫方法检测到无活性的酶蛋白。结合该反应在体内的不可逆性,这一发现强烈提示存在一种酶失活的蛋白水解机制。对于这一过程,使用术语“分解代谢物降解”。