The role of covalently bound fatty acids in the degradation of human gastric mucus glycoprotein.
The role of covalently bound fatty acids in the degradation of human gastric mucus glycoprotein.
复制标题
共价结合脂肪酸在人胃粘液糖蛋白降解中的作用。
DOI:
10.1016/0003-9861(84)90188-7
复制
发表时间:
1984
影响因子:
3.9
通讯作者:
Slomiany,BL
中科院分区:
文献类型:
--
作者:
Slomiany,A;Jozwiak,Z;Takagi,A;Slomiany,BL
The undegraded high-molecular-weight glycoprotein of human gastric mucus has been isolated free of noncovalently bound proteins and lipids, as judged by gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, cesium chloride density gradient centrifugation, and lipid analysis. Mild alkaline methanolysis of the thoroughly delipidated glycoprotein revealed that, on the average, the native undegraded glycoprotein contains 2.9 mol of acyl linked fatty acids/mg glycoprotein. The low-molecular-weight glycoprotein subunits, obtained after pepsin digestion, contain 2 nmol of acyl linked fatty acids/mg glycopeptide. The highest content of covalently bound fatty acids was found in the fraction of glycoprotein which remained undegraded after pepsin digestion. On the average, 10.2 mol of fatty acids/mg was substituted on this pepsin-resistant glycoprotein. After deacylation with hydroxylamine, the undegraded pepsinresistant glycoprotein became susceptible to proteolytic cleavage. The obtained results suggest that fatty acids covalently bound to gastric mucus glycoprotein are involved in the regulation of proteolytic digestion of mucus glycoprotein in the stomach.