Sharma Savita, Gokhale Sadashiv M
Indian J Biochem Biophys. 2014 Oct;51(5):378-87.
Study was carried out to understand and compare architecture of the proteins of erythrocyte cell surface of some mammals viz., Homo sapiens (human), Sus scorfa domestica (pig) and Bos taurus domestica (cow). In this study, we investigated the action of proteinases viz., trypsin and chymotrypsin and neuraminidase on the erythrocyte surface proteins and erythrocyte agglutination tendency with a lectin (concanavalin A). The electrophoretic pattern of membrane proteins and glycophorins (analyzed by SDS-PAGE and visualized by Coomassie brilliant blue and periodic acid-schiff stains, respectively) and concanavalin A (Con A) agglutinability revealed that: (i) There were variations in the number and molecular weights of glycophorins in human, pig and cow, (ii) trypsin action on pig and cow erythrocyte membrane proteins was similar, unlike human, (iii) glycophorins degradation by trypsin and chymotrypsin was not similar in pig, as compared to that of human and cow, (iv) erythrocytes agglutination with Con A was significantly different due to differences in membrane composition and alterations in the surface proteins after enzyme treatment, (v) a direct correlation was found between degradation of glycophorins and Con A agglutinability, and (vi) removal of erythrocyte surface sialic acids by neuraminidase specifically indicated an increase in Con A agglutinability of pig and cow erythrocytes, similar to human.
开展了一项研究，以了解和比较一些哺乳动物（即智人（人类）、家猪和家牛）红细胞细胞表面蛋白质的结构。在本研究中，我们研究了蛋白酶（即胰蛋白酶和糜蛋白酶）和神经氨酸酶对红细胞表面蛋白质的作用，以及凝集素（伴刀豆球蛋白A）对红细胞凝集趋势的影响。膜蛋白和血型糖蛋白的电泳图谱（分别通过SDS-PAGE分析，并用考马斯亮蓝和过碘酸-希夫染色法进行可视化）以及伴刀豆球蛋白A（Con A）的凝集性表明：（i）人类、猪和牛的血型糖蛋白在数量和分子量上存在差异，（ii）胰蛋白酶对猪和牛红细胞膜蛋白的作用相似，与人类不同，（iii）与人类和牛相比，猪的血型糖蛋白被胰蛋白酶和糜蛋白酶降解的情况不同，（iv）由于膜组成的差异以及酶处理后表面蛋白的改变，红细胞与Con A的凝集存在显著差异，（v）发现血型糖蛋白的降解与Con A的凝集性之间存在直接相关性，并且（vi）神经氨酸酶去除红细胞表面唾液酸后，猪和牛红细胞的Con A凝集性显著增加，与人类相似。
