Testa J, Daniel L W, Kreger A S
Infect Immun. 1984 Aug;45(2):458-63. doi: 10.1128/iai.45.2.458-463.1984.
Phospholipase A2 and lysophospholipase activities were detected in the culture supernatant fluids of a virulent strain of Vibrio vulnificus. The phospholipase A2 was inactivated by heating at 56 degrees C for 30 min, had an apparent molecular weight of greater than or equal to 80,000 (estimated by gel filtration with Sephadex G-75), and a pI of ca. 5.0. Phospholipid hydrolysis was unaffected by Ca2+ or ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid and was optimal at pH 5.0 to 5.5. The lysophospholipase was not affected by heating at 56 degrees C for 30 min but was inactivated at 100 degrees C and had an apparent molecular weight of greater than or equal to 80,000 and a pI of ca. 4.0. The enzymes were detected coincidentally with a previously described extracellular cytolysin of V. vulnificus; however, they were physically separable from the toxin (which did not possess phospholipase A, C, or D activity) by gel filtration with Sephadex G-75.
在创伤弧菌的一个强毒株的培养上清液中检测到了磷脂酶A2和溶血磷脂酶活性。磷脂酶A2在56℃加热30分钟后失活，表观分子量大于或等于80,000（通过用葡聚糖G-75进行凝胶过滤估计），pI约为5.0。磷脂水解不受Ca2+或乙二醇双（β-氨基乙醚）-N,N-四乙酸的影响，在pH 5.0至5.5时最适宜。溶血磷脂酶在56℃加热30分钟不受影响，但在100℃失活，表观分子量大于或等于80,000，pI约为4.0。这些酶与先前描述的创伤弧菌细胞外溶素同时被检测到；然而，通过用葡聚糖G-75进行凝胶过滤，它们与毒素（不具有磷脂酶A、C或D活性）在物理上是可分离的。
