Di Cola D, Federici G
Physiol Chem Phys. 1982;14(4):323-6.
Tyrosine aminotransferase from guinea pig liver spontaneously inactivates both in crude homogenates and in tissue slices. In the course of inactivation the cytosolic enzyme progressively translocates only into the microsomal fraction under an inactive form. Translocated enzyme activity can be restored by dithiothreitol addition which also produces the release of the enzyme from the microsomal particles. The specific binding of tyrosine aminotransferase to microsomal particles as a critical event for subsequent proteolytic degradation of the enzyme is postulated.
豚鼠肝脏中的酪氨酸转氨酶在粗匀浆和组织切片中都会自发失活。在失活过程中，胞质酶仅以无活性形式逐渐转位到微粒体部分。通过添加二硫苏糖醇可以恢复转位酶的活性，二硫苏糖醇还能使酶从微粒体颗粒中释放出来。推测酪氨酸转氨酶与微粒体颗粒的特异性结合是该酶随后发生蛋白水解降解的关键事件。
