Swendeman S, Thorley-Lawson D A
EMBO J. 1987 Jun;6(6):1637-42. doi: 10.1002/j.1460-2075.1987.tb02412.x.
A shed form of the membrane-bound B cell activation marker, BLAST-2 (Epstein-Barr virus cell surface, CD 23) was immune-affinity purified from Epstein-Barr virus-transformed lymphoblast conditioned medium. SDS-PAGE analysis revealed a complex of two polypeptides, mol. wts 25,000 and 12,000, here termed s-BLAST-2. We show that this complex, when purified to homogeneity, can act as a growth factor for EBV-infected B lymphoblasts and normal receptor-stimulated B cell blasts. It has no effect on resting B or T cells. These data suggest that the BLAST-2 antigen has a role in autocrine B cell growth. Additionally, this complex is a co-mitogen for PHA-stimulated murine thymocytes, a property of interleukin-1.
从爱泼斯坦-巴尔病毒转化的淋巴母细胞条件培养基中免疫亲和纯化出一种膜结合型B细胞活化标志物BLAST-2（爱泼斯坦-巴尔病毒细胞表面，CD 23）的 shed 形式。SDS-PAGE分析显示有两种分子量分别为25,000和12,000的多肽形成的复合物，此处称为s-BLAST-2。我们发现，这种纯化至均一的复合物可作为爱泼斯坦-巴尔病毒感染的B淋巴母细胞和正常受体刺激的B细胞母细胞的生长因子。它对静止的B细胞或T细胞没有作用。这些数据表明BLAST-2抗原在自分泌B细胞生长中起作用。此外，这种复合物是PHA刺激的小鼠胸腺细胞的共促有丝分裂原，这是白细胞介素-1的一种特性。
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