Ishioka N, Kurioka S
Division of Biochemistry, Jikei University School of Medicine, Tokyo, Japan.
Neurochem Res. 1992 Oct;17(10):1011-4. doi: 10.1007/BF00966829.
Concanavalin A (Con A)-binding proteins obtained from solubilized synaptosomal membranes of bovine brain were analyzed by two-dimensional electrophoresis (2DE), and were identified by peroxidase conjugated Con A (Con A-peroxidase staining), after transfer from 2DE gel to nitrocellulose paper. The Con A-binding proteins were resolved up to 40 spots, ranging in isoelectric points (pI) from 4.5 to 8.0 and molecular weight (MW) from 10 kDa to 120 kDa. Most of the Con A-binding proteins were streaked across a pH gradient and/or exhibited as multiple spots, indicating broad charge and molecular weight heterogeneity. The presence of protein groups that showed high affinities for Con A were revealed. Most interesting group (named GP51), which consisted of seven spots separated horizontally in charge heterogeneity (pI5.85-7.5) with MW 51 kDa, was characterized by its binding to an immobilized protein A gel. This implies that GP51 is related to immunoglobulins and/or GP51 may be a new member of the immunoglobulin supergene family.
从牛脑可溶突触体膜中获得的伴刀豆球蛋白A（Con A）结合蛋白，通过二维电泳（2DE）进行分析，并在从2DE凝胶转移至硝酸纤维素纸后，用过氧化物酶偶联的Con A（Con A-过氧化物酶染色）进行鉴定。Con A结合蛋白可分辨出多达40个斑点，等电点（pI）范围为4.5至8.0，分子量（MW）范围为10 kDa至120 kDa。大多数Con A结合蛋白在pH梯度上呈条纹状分布和/或表现为多个斑点，表明电荷和分子量具有广泛的异质性。揭示了对Con A具有高亲和力的蛋白质组的存在。最有趣的一组（命名为GP51）由七个斑点组成，这些斑点在电荷异质性（pI 5.85 - 7.5）中水平分离，分子量为51 kDa，其特征是与固定化蛋白A凝胶结合。这意味着GP51与免疫球蛋白有关，和/或GP51可能是免疫球蛋白超基因家族的一个新成员。
