Endo J, Otsuka M, Ohara E, Sato M, Nakamura R
Department of Preventive Dentistry, School of Dentistry, University of Tokushima, Japan.
Arch Oral Biol. 1989;34(11):911-6. doi: 10.1016/0003-9969(89)90149-0.
Soluble reduced lysozyme was extensively digested by a trypsin-like protease purified from the culture supernatant of the bacterium. The digestion peptides were separated and purified by reversed-phase high-performance liquid chromatography, and were subjected to amino acid analysis. The fragments were identified by their amino acid composition, and the cleavage sites in the lysozyme chain were determined. Like mammalian trypsin, the enzyme from B. gingivalis split peptide bonds non-specifically at carboxyl sides of internal arginine and lysine residues, but the lysine present at the amino terminus of the lysozyme chain was not released. In addition, the enzyme cleaved the peptide linkage at the amino side of lysine and bonds between leucine-glycine, alanine-leucine and leucine-serine. Thus the trypsin-like protease from B. gingivalis has some cleavage actions on lysozyme different from those of mammalian trypsin.
可溶性还原溶菌酶被从该细菌培养上清液中纯化得到的一种类胰蛋白酶广泛消化。消化后的肽段通过反相高效液相色谱进行分离和纯化，并进行氨基酸分析。通过氨基酸组成鉴定片段，并确定溶菌酶链中的裂解位点。与哺乳动物胰蛋白酶一样，牙龈卟啉单胞菌的这种酶在内部精氨酸和赖氨酸残基的羧基侧非特异性地裂解肽键，但溶菌酶链氨基末端的赖氨酸不会被释放。此外，该酶还能在赖氨酸的氨基侧裂解肽键以及亮氨酸 - 甘氨酸、丙氨酸 - 亮氨酸和亮氨酸 - 丝氨酸之间的肽键。因此，牙龈卟啉单胞菌的类胰蛋白酶对溶菌酶具有一些不同于哺乳动物胰蛋白酶的裂解作用。
