Zeya H I, Spitznagel J K
J Exp Med. 1968 May 1;127(5):927-41. doi: 10.1084/jem.127.5.927.
The cationic antibacterial proteins of rabbit PMN lysosomes have been resolved into at least five subfractions. Each of these showed substantial selectivity in its antibacterial action against several pathogenic bacteria, including two smooth and two rough Escherichia coli strains, three Staphylococcus aureus strains, one S. albus, three proteus species and four different cultures of streptococcus. Each of the subfractions possesses a different electrophoretic mobility. Amino acid analyses of the three most cationic components revealed high contents of arginine consistent with their relative electrophoretic mobilities and very high arginine to lysine ratios. Aromatic amino acids were present in very low concentrations in these proteins and their light absorption at 2800 A was correspondingly weak. The evidence of antibacterial specificity, along with marked differences in the arginine-lysine ratios, shows that the cationic antibacterial components of rabbit PMN lysosomes are biologically and chemically heterogeneous.
兔中性粒细胞溶酶体的阳离子抗菌蛋白已被分离成至少五个亚组分。其中每一个亚组分在对几种病原菌的抗菌作用上都表现出显著的选择性，这些病原菌包括两种光滑型和两种粗糙型大肠杆菌菌株、三种金黄色葡萄球菌菌株、一种白色葡萄球菌、三种变形杆菌属菌种以及四种不同培养的链球菌。每个亚组分都具有不同的电泳迁移率。对三种阳离子性最强的组分进行氨基酸分析发现，精氨酸含量很高，这与其相对电泳迁移率相符，且精氨酸与赖氨酸的比例非常高。这些蛋白质中芳香族氨基酸的浓度极低，因此它们在2800埃处的光吸收相应较弱。抗菌特异性的证据以及精氨酸 - 赖氨酸比例的显著差异表明，兔中性粒细胞溶酶体的阳离子抗菌组分在生物学和化学性质上是异质的。
