中性匀浆和大鼠肝切片中酪氨酸转氨酶的失活
Inactivation of tyrosine aminotransferase in neutral homogenates and rat liver slices.
作者信息
Auricchio F, Mollica L, Liguori A
出版信息
Biochem J. 1972 Oct;129(5):1131-8. doi: 10.1042/bj1291131.
Inactivation of tyrosine aminotransferase induced in vivo by triamcinolone was studied in a homogenate incubated at neutral pH values. The integrity and the presence of subcellular particles together with a compartment of acidic pH are necessary for inactivation of tyrosine aminotransferase. It is suggested that tyrosine aminotransferase is inactivated inside lysosomes. The system responsible for inactivation of tyrosine aminotransferase was partially purified and identified with lysosomal cathepsins B and B(1). Inactivation of tyrosine aminotransferase in liver slices is controlled by the amino acid concentration and strongly stimulated by cysteine. 3,3',5-Tri-iodo-l-thyronine reversibly and strongly decreases the rate of inactivation of tyrosine aminotransferase. The effect is not due to an increased rate of tyrosine aminotransferase synthesis.
在中性pH值下孵育的匀浆中研究了曲安西龙在体内诱导的酪氨酸转氨酶失活情况。酪氨酸转氨酶失活需要亚细胞颗粒的完整性和酸性pH区室的存在。提示酪氨酸转氨酶在溶酶体内失活。负责酪氨酸转氨酶失活的系统被部分纯化，并鉴定为溶酶体组织蛋白酶B和B(1)。肝切片中酪氨酸转氨酶的失活受氨基酸浓度控制，并受到半胱氨酸的强烈刺激。3,3',5-三碘-L-甲状腺原氨酸可逆且强烈地降低酪氨酸转氨酶的失活速率。该效应并非由于酪氨酸转氨酶合成速率增加所致。
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