Liau Y H, Slomiany B L, Slomiany A, Piasek A, Palmer D, Rosenthal W S
Digestion. 1985;32(1):57-62. doi: 10.1159/000199218.
The enzymatic activity which catalyzes the transfer of palmitic acid from palmitoyl coenzyme A to gastric mucus glycoprotein was demonstrated in antral and fundic mucosa of normal human stomach. Subcellular fractionation studies revealed that with both types of mucosa the enzyme activity was present in the microsomal fraction. The antral and fundic mucosa also exhibited similar enzyme activities, showed identical pH optimum, and required detergent, NaF and dithiothreitol. Optimum enzymatic activity for fatty acylation of mucus glycoprotein was obtained with 0.5% Triton X-100, 25 mM NaF, and 2 mM dithiothreitol at a pH of 7.4. The 14C-labeled product of the reaction comigrated on CsCl density gradient centrifugation with gastric mucus glycoprotein and contained the ester-bound palmitic acid.
在正常人体胃的胃窦和胃底黏膜中，证实了催化棕榈酸从棕榈酰辅酶A转移至胃黏液糖蛋白的酶活性。亚细胞分级分离研究表明，两种类型的黏膜中，该酶活性均存在于微粒体部分。胃窦和胃底黏膜还表现出相似的酶活性，具有相同的最适pH值，且需要去污剂、氟化钠和二硫苏糖醇。在pH值为7.4时，使用0.5% Triton X-100、25 mM氟化钠和2 mM二硫苏糖醇可获得黏液糖蛋白脂肪酰化的最佳酶活性。反应的14C标记产物在氯化铯密度梯度离心中与胃黏液糖蛋白共迁移，并含有酯结合的棕榈酸。
