ELECTROPHORETIC DETECTION OF PROTEASES FROM DIFFERENT FLEXIBACTER-COLUMNARIS STRAINS AND ASSESSMENT OF THEIR VARIABILITY
ELECTROPHORETIC DETECTION OF PROTEASES FROM DIFFERENT FLEXIBACTER-COLUMNARIS STRAINS AND ASSESSMENT OF THEIR VARIABILITY
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DOI：
10.3354/dao012121
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发表时间：
1992-02-17
影响因子：
1.4
通讯作者：
ROHOVEC, JS
中科院分区：
文献类型：
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作者：
BERTOLINI, JM;ROHOVEC, JS
采用底物SDS-聚丙烯酰胺凝胶电泳技术，从柱状假单胞菌胞外产物（ECP）中鉴定出表观分子量为47、40、34和32 kD的蛋白酶。 类似的蛋白酶谱与培养物中几天内间隔收集的ECP相关。 此外，还对13株F.从各种鱼类和地理来源分离的柱状细菌显示出很大的一致性，但与所检测的其他7种滑行细菌的蛋白酶谱明显不同。 13 F。柱状分离物降解明胶、酪蛋白、血红蛋白、纤维蛋白原和弹性蛋白。 蛋白酶抑制剂的实验结果表明，锌金属蛋白酶构成的胞外蛋白酶的主要组成部分的F。圆柱形。
Proteases with apparent molecular weights of 47, 40, 34 and 32 kD were identified in cell-free extracellular products (ECP) of Flexibacter columnaris by using substrate SDS-polyacrylamide gel electrophoresis. Similar protease profiles were associated with ECP collected at intervals during several days in culture. Furthermore, the proteases produced by a collection of 13 F. columnaris isolates from a variety of fish species and geographic sources showed great uniformity but differed markedly from the protease profiles of 7 other gliding bacteria examined. The 13 F. columnaris isolates degraded gelatin, casein, hemoglobin, fibrinogen and elastin. Results of experiments with protease inhibitors indicated that zinc metalloproteases constitute a major component of the extracellular proteases of F. columnaris.