Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/17183
Title: Heat modifiability of outer membrane protein of Pasteurella multocida serotype B:2
Authors: Pal, Anirban
Srivastava, S K
Singh, V P
Issue Date: Jan-2002
Publisher: NISCAIR-CSIR, India
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 ~39 and~28 kDa were found to be heat modifiable. It is suggested that boiling at 100°C in presence of β mercaptoethanol for 5 min is sufficient for characterisation of OMP by Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis.
Page(s): 106-108
URI: http://hdl.handle.net/123456789/17183
ISSN: 0975-1009 (Online); 0019-5189 (Print)
Appears in Collections:IJEB Vol.40(01) [January 2002]

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