Sharma Savita, Punjabi Vinny, Zingde Surekha M, Gokhale Sadashiv M
School of Biochemistry, Devi Ahilya University, Khandwa Road, Indore, 452017, India.
J Membr Biol. 2014 Nov;247(11):1181-9. doi: 10.1007/s00232-014-9718-0. Epub 2014 Aug 24.
A comparative analysis of erythrocyte membrane proteins of economically important animals, goat (Capra aegagrus hircus), buffalo (Bubalus bubalis), pig (Sus scrofa), cow (Bos tauras), and human (Homo sapiens) was performed. Solubilized erythrocyte membrane proteins were separated by sodium dodecyl sulfate-polyacryamide gel electrophoresis (SDS-PAGE), visualized by staining the gels with Commassie Brilliant Blue (CBB), and identified by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS). Emerging results show that all major erythrocyte membrane proteins present in human are also seen in all the animals except for band 4.5 which could not be identified. Band 3 is seen as more intense and compact, band 4.1 appears as a doublet in all the animal erythrocyte membranes, band 4.2 exhibits a slightly higher molecular weight (Mr) in buffalo, and cow and band 4.9 has a higher Mr in all the animals relative to the human protein. In addition, there are two new bands in the goat membrane, band G1, identified as HSP 90α, and band G2 identified as HSP 70. A new band C2 identified as HSP 70 is also seen in cow membranes. Peroxiredoxin II is of lower intensity and/or higher Mr in the animals. The difference in size of the proteins possibly indicates the variations in the composition of the amino acids. The difference in intensity of the proteins among these mammalians highlights the presence of less or more number of copies of that protein per cell. This data complement the earlier observations of differences in the sialoglycoprotein profile and effect of proteases and neuraminidase on agglutination among the mammalian erythrocytes. This study provides a platform to understand the molecular architecture of the individual erythrocytes, and in turn the dependent disorders, their phylogenetic relationship and also generates a database of erythrocyte membrane proteins of mammals. The animals selected for this study are of economic importance as they provide milk for the dairy industry and raw material for leather industry and are routinely sacrificed to obtain non vegetarian food worldwide.
对具有经济重要性的动物,即山羊(Capra aegagrus hircus)、水牛(Bubalus bubalis)、猪(Sus scrofa)、奶牛(Bos tauras)和人类(Homo sapiens)的红细胞膜蛋白进行了比较分析。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)分离溶解的红细胞膜蛋白,用考马斯亮蓝(CBB)对凝胶进行染色以可视化,并通过基质辅助激光解吸电离飞行时间质谱(MALDI-TOF/MS)进行鉴定。新出现的结果表明,除了无法鉴定的4.5条带外,人类中存在的所有主要红细胞膜蛋白在所有动物中也都可见。3条带看起来更密集且紧密,4.1条带在所有动物红细胞膜中表现为双峰,4.2条带在水牛、奶牛中的分子量(Mr)略高,4.9条带在所有动物中的Mr相对于人类蛋白更高。此外,山羊膜中有两条新带,G1带被鉴定为热休克蛋白90α(HSP 90α),G2带被鉴定为热休克蛋白70(HSP 70)。在奶牛膜中也可见一条被鉴定为HSP 70的新带C2。过氧化物酶II在动物中的强度较低和/或Mr较高。蛋白质大小的差异可能表明氨基酸组成的变化。这些哺乳动物中蛋白质强度的差异突出了每个细胞中该蛋白质拷贝数的或多或少。这些数据补充了早期关于哺乳动物红细胞中唾液糖蛋白谱差异以及蛋白酶和神经氨酸酶对凝集作用影响的观察结果。本研究提供了一个平台,以了解单个红细胞的分子结构,进而了解相关疾病、它们的系统发育关系,还生成了哺乳动物红细胞膜蛋白数据库。本研究选择的动物具有经济重要性,因为它们为乳制品行业提供牛奶,为皮革行业提供原材料,并且在全球范围内经常被宰杀以获取非素食食品。