Crossed immunoelectrophoresis, in the presence of tween 20 or sodium deoxycholate, of purified membrane proteins from Acholeplasma laidlawii. |
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Authors: | K E Johansson and H Wrblewski |
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Institution: | K E Johansson and H Wróblewski |
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Abstract: | Five membrane proteins from Acholeplasma laidlawii have been previously purified on a large scale. These proteins have been used to establish the relationship between the precipitation lines obtained by crossed immunoelectrophoresis of solubilized cell membrane proteins from A. laidlawii in the presence of the neutral detergent Tween 20 or those obtained in the presence of the anionic detergent sodium deoxycholate. This relationship, which was unambiguously established for four of the five proteins, was determined by tandem or "parallel" crossed immunoelectrophoresis of the sodium deoxycholate-solubilized membrane together with the purified proteins. Membranes from strain A of A. laidlawii were composed of proteins, which were immunologically related to and probably identical to membrane proteins from strain B of this organism. |
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