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多杀性巴氏杆菌B:2型外膜蛋白的热可修饰性

Heat modifiability of outer membrane protein of Pasteurella multocida serotype B:2.

作者信息

Pal Anirban, Srivastava S K, Singh V P

机构信息

Division of Bacteriology and Mycology, Indian Veterinary Research Institute, Izatnagar 243 122, India.

出版信息

Indian J Exp Biol. 2002 Jan;40(1):106-8.

Abstract

Outer membrane proteins (OMP) are generally porins, functioning as molecular sieves assisting in the transmembrane transportation. Heat modifiable characteristics of OMP from P. multocida B: 2 have been explored to know their basic characteristics on event of temperature rise. A major band of 32 kDa and two minor bands of approximately 39 and approximately 28 kDa were found to be heat modifiable. It is suggested that boiling at 100 degrees C in presence of beta mercaptoethanol for 5 min is sufficient for characterisation of OMP by Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis.

摘要

外膜蛋白(OMP)通常是孔蛋白,作为分子筛协助跨膜运输。已对多杀性巴氏杆菌B:2的OMP的热可修饰特性进行了研究,以了解其在温度升高时的基本特性。发现一条32 kDa的主要条带以及两条约39 kDa和约28 kDa的次要条带具有热可修饰性。建议在存在β-巯基乙醇的情况下于100℃煮沸5分钟,足以通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳对OMP进行表征。

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