Ishibashi Y, Yamashita T
Infect Immun. 1985 Jun;48(3):799-805. doi: 10.1128/iai.48.3.799-805.1985.
Phagocytosis-stimulating factor (PSF) was purified by copper chelate chromatography and characterized in comparison with basic proteins in the granule of polymorphonuclear neutrophils. By copper chelate chromatography, PSF was eluted at pH 3.7; whereas cationic protein, lysozyme, and lactoferrin were eluted at pH 5.6, 5.1, and 4.0, respectively. Purified PSF has an approximate molecular weight of 16,000 and an isoelectric point at 8.7, which differ from those of basic proteins, such as cationic protein, lysozyme, and lactoferrin. Anionic substances such as DNA and heparin did not influence the phagocytosis-stimulating activity of PSF, whereas that of the granule basic protein fraction from resting polymorphonuclear neutrophils was abolished. PSF had little bactericidal activity against Escherichia coli and Staphylococcus aureus, whereas the granule basic protein fraction from resting PMNs had strong bactericidal activity against E. coli and weak activity against S. aureus. These results indicate that PSF is a basic protein which is distinguishable from cationic protein, lysozyme, and lactoferrin.
通过铜螯合层析法纯化吞噬刺激因子（PSF），并与多形核中性粒细胞颗粒中的碱性蛋白进行比较表征。通过铜螯合层析法，PSF在pH 3.7时洗脱；而阳离子蛋白、溶菌酶和乳铁蛋白分别在pH 5.6、5.1和4.0时洗脱。纯化的PSF的近似分子量为16,000，等电点为8.7，这与阳离子蛋白、溶菌酶和乳铁蛋白等碱性蛋白不同。DNA和肝素等阴离子物质不影响PSF的吞噬刺激活性，而静息多形核中性粒细胞颗粒碱性蛋白组分的吞噬刺激活性则被消除。PSF对大肠杆菌和金黄色葡萄球菌几乎没有杀菌活性，而静息多形核白细胞的颗粒碱性蛋白组分对大肠杆菌有很强的杀菌活性，对金黄色葡萄球菌有较弱的活性。这些结果表明，PSF是一种与阳离子蛋白、溶菌酶和乳铁蛋白不同的碱性蛋白。
