Morse S A, Mietzner T A, Bolen G, Le Faou A, Schoolnik G
Centers for Disease Control, Sexually Transmitted Diseases Laboratory Program, Atlanta, GA 30333.
Antonie Van Leeuwenhoek. 1987;53(6):465-9. doi: 10.1007/BF00415504.
The major iron-regulated protein (MIRP) was purified, from both Neisseria gonorrhoeae and N. meningitidis by selective extraction with cetyltrimethylammonium bromide followed by ion-exchange and moleculair-seive chromatography. Solutions of the purified proteins had a characteristic pink color. The overall amino acid composition of these proteins was similar, although differences were noted in the number of serine, threonine, and lysine residues. Nevertheless, the N-terminal amino acid sequence was identical through 47 residues for both the meningococcal and gonococcal MIRP. Plasma emission spectrophotometry revealed that the meningococcal 37K protein contained ca. 1 mole Fe/mole protein.
主要铁调节蛋白（MIRP）通过用十六烷基三甲基溴化铵选择性提取，随后进行离子交换和分子筛色谱法，从淋病奈瑟菌和脑膜炎奈瑟菌中纯化得到。纯化蛋白溶液呈现出特有的粉红色。尽管这些蛋白在丝氨酸、苏氨酸和赖氨酸残基数量上存在差异，但其整体氨基酸组成相似。然而，脑膜炎球菌和淋病球菌的MIRP在47个残基范围内的N端氨基酸序列是相同的。等离子体发射光谱法显示，脑膜炎球菌的37K蛋白每摩尔蛋白约含1摩尔铁。
