Ben-Yoseph Y, Potier M, Pack B A, Mitchell D A, Melançon S B, Nadler H L
Biochem J. 1986 May 1;235(3):883-6. doi: 10.1042/bj2350883.
The radiation inactivation method was used to determine the molecular size of the two enzymes that participate in the synthesis of the phosphomannosyl recognition marker of lysosomal proteins. The determinations were carried out in situ, in Golgi membranes isolated from normal human placenta and cultured skin fibroblasts. A molecular size of 228 +/- 29 kDa was found for placental N-acetylglucosaminyl-phosphotransferase, and 129 +/- 11 kDa for placental alpha-N-acetylglucosaminyl phosphodiesterase. The values for the fibroblast enzymes were about 20% higher, 283 +/- 27 kDa and 156 +/- 14 kDa for the transferase and phosphodiesterase respectively. Triton X-100 had no effect on the molecular size of these enzymes.
采用辐射失活法测定参与溶酶体蛋白磷酸甘露糖识别标记合成的两种酶的分子大小。测定是在原位进行的,所用的高尔基体膜取自正常人胎盘和培养的皮肤成纤维细胞。胎盘N-乙酰葡糖胺磷酸转移酶的分子大小为228±29 kDa,胎盘α-N-乙酰葡糖胺磷酸二酯酶的分子大小为129±11 kDa。成纤维细胞中这两种酶的值分别约高20%,转移酶为283±27 kDa,磷酸二酯酶为156±14 kDa。Triton X-100对这些酶的分子大小没有影响。