Böhmer F D, Kirschke H, Bohley P, Schön R
Acta Biol Med Ger. 1979;38(11-12):1521-6.
The capacity of membrane glycoproteins to interact with proteinases was investigated in the model system: Membrane sialoglycoprotein from human erythrocytes (glycophorin) and lysosomal proteinases from rat liver. Glycophorin was found to stimulate the activity of a lysosomal proteinase mixture up to about 150% at pH 6.9. Cathepsin L was found to be the primarily stimulated proteinase. The stoichiometry in the saturation range of the dose-response curve waas about 10 to 20 molecules glycophorin per molecule cathepsin L. The mechanism of the activation is unknown. Interactions of this type may be of importance for the regulation of cell proliferation on the level of cell membranes.
来自人红细胞的膜唾液酸糖蛋白（血型糖蛋白）和来自大鼠肝脏的溶酶体蛋白酶。发现在pH 6.9时，血型糖蛋白可将溶酶体蛋白酶混合物的活性刺激至约150%。发现组织蛋白酶L是主要受刺激的蛋白酶。剂量反应曲线饱和范围内的化学计量比约为每分子组织蛋白酶L对应10至20个血型糖蛋白分子。激活机制尚不清楚。这种类型的相互作用可能在细胞膜水平上对细胞增殖的调节具有重要意义。
