title: Heat modifiability of outer membrane protein of Pasteurella multocida serotype B:2.
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.
authors.affiliation: Division of Bacteriology and Mycology, Indian Veterinary Research Institute, Izatnagar 243 122, India. drapaul@yahoo.com
authors.forename: Anirban
authors.initials: A
authors.lastname: Pal
authors.forename: S K
authors.initials: SK
authors.lastname: Srivastava
authors.forename: V P
authors.initials: VP
authors.lastname: Singh
mesh_terms: D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D051379:Mice; D016979:Pasteurella multocida / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification
chemical_list: D001425:Bacterial Outer Membrane Proteins