Glucagon-stimulated phosphorylation of mitochondrial and lysosomal membranes of rat liver in vivo.
Glucagon-stimulated phosphorylation of mitochondrial and lysosomal membranes of rat liver in vivo.
复制标题
胰高血糖素刺激体内大鼠肝脏线粒体和溶酶体膜的磷酸化。
DOI：
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发表时间：
1972
影响因子：
11.1
通讯作者：
H. Lardy
中科院分区：
文献类型：
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作者：
R. Zahlten;A. Hochberg;F. Stratman;H. Lardy
胰腺激素，胰升糖素，在体内刺激大鼠肝脏对无机(32)P的净摄取，并将其并入微粒体、线粒体膜和溶酶体的蛋白质中。胰升糖素对胞浆蛋白的掺入只有轻微的促进作用。95%以上的蛋白质结合的磷酸盐以磷酸丝氨酸的形式存在。注射胰高血糖素后，放射性和蛋白结合磷酸盐总量均增加。经胰升糖素处理后，~(32)P掺入线粒体醇醚可溶脂中的比例增加，但不改变~(32)P在各种磷脂中的相对分布。
The pancreatic hormone, glucagon, stimulates the net uptake of inorganic (32)P in vivo into rat liver and its incorporation into proteins of microsomes, mitochondrial membranes, and lysosomes. Incorporation into cytosolic proteins was enhanced only slightly by glucagon. More than 95% of the protein-bound phosphate is present as phosphoserine. Both the radioactivity and the total amount of protein-bound phosphate are increased after injection of glucagon. Glucagon treatment enhanced (32)P incorporation into the alcohol-ether soluble lipids of mitochondria but did not alter the relative distribution of (32)P in various phospholipid species.