The sidedness of carnitine acetyltransferase and carnitine octanoyltransferase of rat liver endoplasmic reticulum.
The sidedness of carnitine acetyltransferase and carnitine octanoyltransferase of rat liver endoplasmic reticulum.
复制标题
大鼠肝内质网肉碱乙酰转移酶和肉碱辛酰转移酶的侧面性。
DOI:
10.1016/0005-2736(82)90190-0
复制
发表时间:
1982
期刊:
影响因子:
--
通讯作者:
Bieber,LL
中科院分区:
文献类型:
--
作者:
Valkner,KJ;Bieber,LL
The location of carnitine acetyltransferase and carnitine octanoyltransferase on the inner and outer surfaces of rat liver microsomes was investigated. Latency of mannose-6-phosphate phosphatase showed that the microsomes were 90–94% sealed. All of the octanoyltransferase is associated with the cytosolic face, while the acetyltransferase is distributed between the cytosolic face (68–73%) and the lumen face (27–32%) of the endoplasmic reticulum membrane. Small amounts of trypsin inhibit the carnitine octanoyltransferase equally in either sealed or permeable microsomes but the acetyltransferase of sealed microsomes is stimulated. Large amounts of trypsin inhibit all transferase activities by about 60%, except for acetyltransferase of sealed microsomes. Other studies show that 0.1% Triton X-100 partially inhibits carnitine octanoyltransferase of microsomes but does not inhibit the acetyltransferase or any of the mitochondrial carnitine acyltransferase.