鱼精蛋白对牙龈卟啉单胞菌蛋白水解活性和黏附活性的抑制作用。
Inhibitory effects of protamines on proteolytic and adhesive activities of Porphyromonas gingivalis.
作者信息
Kontani M, Amano A, Nakamura T, Nakagawa I, Kawabata S, Hamada S
机构信息
Department of Oral Microbiology, Osaka University Faculty of Dentistry, Suita-Osaka 565-0871, Japan.
出版信息
Infect Immun. 1999 Sep;67(9):4917-20. doi: 10.1128/IAI.67.9.4917-4920.1999.
Abstract
Protamines (salmine prepared from sperm DNA of salmon and clupeine from herring sperm), which are basic peptides rich in arginine, were found to inhibit the proteolytic activity of arginine-specific cysteine protease (RC-protease) from Porphyromonas gingivalis. Lineweaver-Burk plot analysis revealed that the protamines competitively inhibited proteolytic activity with cleavage of benzoyl-L-arginine-p-nitroanilide, a synthetic substrate of RC-protease. Furthermore, the protamines were capable of binding strongly to P. gingivalis fimbriae and inhibited fimbrial interaction with immobilized fibronectin. These results clearly show that protamines are potent inhibitors of the proteolytic and adhesive activities of P. gingivalis.
摘要
鱼精蛋白（从鲑鱼精子DNA制备的鲑精蛋白和从鲱鱼精子制备的鲱精蛋白）是富含精氨酸的碱性肽，已发现其可抑制牙龈卟啉单胞菌精氨酸特异性半胱氨酸蛋白酶（RC-蛋白酶）的蛋白水解活性。Lineweaver-Burk作图分析表明，鱼精蛋白通过切割RC-蛋白酶的合成底物苯甲酰-L-精氨酸-对硝基苯胺竞争性抑制蛋白水解活性。此外，鱼精蛋白能够与牙龈卟啉单胞菌菌毛强烈结合，并抑制菌毛与固定化纤连蛋白的相互作用。这些结果清楚地表明，鱼精蛋白是牙龈卟啉单胞菌蛋白水解和黏附活性的有效抑制剂。
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