Scisłowski P W, Zołnierowicz S, Swierczynski J, Elewski L
Biochem Med. 1983 Oct;30(2):141-5. doi: 10.1016/0006-2944(83)90080-7.
It has been shown that L-leucine is transaminated in the presence of 2-oxoglutarate and subsequently decarboxylated by human term placenta. About 60% of the transaminase activity was recovered in the cytoplasmic fraction and the remaining amount in the mitochondria. The dehydrogenase activity is localized almost exclusively in the mitochondrial fraction. The rate of the transamination of L-leucine is many times higher than the rate of decarboxylation of oxoacid. The possible physiological role of leucine degradation in human placenta is discussed.
已经表明，L-亮氨酸在2-氧代戊二酸存在下进行转氨作用，随后被足月人胎盘脱羧。约60%的转氨酶活性存在于细胞质部分，其余部分存在于线粒体中。脱氢酶活性几乎完全定位于线粒体部分。L-亮氨酸的转氨速率比氧代酸的脱羧速率高很多倍。本文讨论了亮氨酸降解在人胎盘中可能的生理作用。
