The effect of neutral lipids, glycolipids and phospholipids associated with dog gastric mucus glycoprotein, and that of covalently bound fatty acids on the ability of glycoprotein to retard the diffusion of hydrogen ion was investigated. Purified mucus glycoprotein in its native form, placed between equimolar (0.155M) solutions of HCl and NaCl in a specially designed two-compartment chamber, caused a 90% reduction in permeability to hydrogen ion when compared with a layer of NaCl. Extraction of associated lipids lead to a 68% increase in permeability of the glycoprotein to hydrogen ion, while removal of the covalently bound fatty acids increased further the diffusion rate by 6%. Reassociation of the delipidated glycoprotein with its neutral lipids reduced the permeability to hydrogen ion by 34%, an 11% reduction was obtained with glycolipids, and 23% with phospholipids. Since neutral lipids account for 47% of the glycoprotein lipids, glycolipids 41.1% and phospholipids 11.9%, the quantitative decrease in permeability of the delipidated glycoprotein following its reassociation with phospholipids is 2.7 times greater than that of neutral lipids and 7.3 times greater than that of glycolipids.
|Original language||English (US)|
|Number of pages||9|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jan 30 1984|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology