Ishibashi Y, Yamashita T
Infect Immun. 1985 Nov;50(2):500-5. doi: 10.1128/iai.50.2.500-505.1985.
A precursor of phagocytosis-stimulating factor (PSF) was identified by immunoblot assay with purified anti-PSF antibodies. The purified anti-PSF antibodies recognized not only the PSF with a molecular weight of 16,000 (16K) but also the 36K protein with a pI of 6.5 in the granule fraction of polymorphonuclear neutrophils, indicating that this 36K protein has an antigenic determinant common to PSF. In addition, the appearance of the PSF during phagocytosis by polymorphonuclear neutrophils was closely correlated to the decrease of the 36K protein. These results suggest that the 36K protein is the precursor of PSF which is converted to biologically active PSF in the granules during phagocytosis.
通过用纯化的抗吞噬刺激因子(PSF)抗体进行免疫印迹分析,鉴定出了吞噬刺激因子(PSF)的前体。纯化的抗PSF抗体不仅识别分子量为16,000(16K)的PSF,还识别多形核中性粒细胞颗粒部分中pI为6.5的36K蛋白,这表明该36K蛋白具有与PSF共有的抗原决定簇。此外,多形核中性粒细胞吞噬过程中PSF的出现与36K蛋白的减少密切相关。这些结果表明,36K蛋白是PSF的前体,在吞噬过程中在颗粒中转化为具有生物活性的PSF。