Berthillier G, Got R
C R Seances Soc Biol Fil. 1979;173(5):927-31.
An activity UTP : D-glucose-1-phosphate uridylyltransferase is located in the microsomal membranes of conger liver. The properties of this enzyme are studied and compared to the soluble activity. The microsomal activity is partially liberated from the membrane by freezing and thawing and by the means of a neutral detergent, Triton X-100. The enzyme is latent in the membranes and totally inhibited by phospholipase A2. This microsomal enzyme could be the last of a membranous biosynthetic pathway for UDP-glucose, as conger liver microsomes contain also a membranous glucokinase and a membranous phosphoglucomutase.
一种活性UTP:D-葡萄糖-1-磷酸尿苷酰转移酶存在于康吉鳗肝脏的微粒体膜中。对该酶的性质进行了研究,并与可溶性活性进行了比较。通过冻融和使用中性去污剂Triton X-100,微粒体活性可部分从膜中释放出来。该酶在膜中呈潜伏状态,并且被磷脂酶A2完全抑制。由于康吉鳗肝脏微粒体中还含有一种膜性葡萄糖激酶和一种膜性磷酸葡萄糖变位酶,这种微粒体酶可能是UDP-葡萄糖膜生物合成途径的最后一步。