A群化脓性链球菌肾炎菌株相关蛋白的纯化及部分特性分析
Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A.
作者信息
Johnston K H, Zabriskie J B
出版信息
J Exp Med. 1986 Mar 1;163(3):697-712. doi: 10.1084/jem.163.3.697.
Abstract
We report the isolation and purification of the nephritis strain-associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis.
摘要
我们报道了对肾炎菌株相关蛋白（NSAP）的分离和纯化，该蛋白最初由比利亚雷亚尔等人描述（8）。氨基酸分析以及对前21个氨基末端氨基酸的测定表明，这种46 kD的蛋白质是一种链激酶。生化分析证实NSAP可作为纤溶酶原激活剂；免疫学研究表明，NSAP在抗原性上与C组链球菌的链激酶不同，可能代表一种独特的链激酶。正是这种独特性可能导致NSAP在急性链球菌感染后肾小球肾炎发病机制中发挥作用。
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Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A.A群化脓性链球菌肾炎菌株相关蛋白的纯化及部分特性分析
J Exp Med. 1986 Mar 1;163(3):697-712. doi: 10.1084/jem.163.3.697.
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