ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
The hydrophobic protein comprising the gas vacuoles of a variety of procaryotic microorganisms is insoluble in detergents (e.g. sodium dodecyl sulfate) and cannot be electrophoresed in detergent-containing systems. The protein is solubilized by mixtures of phenol-acetic acid-urea (PAU) and the development of a slab gel system containing PAU which successfully separates the gas vacuole protein is described. In the system, phenol is polymerized directly into the gel, and the high background staining which results can be minimized by the proper choice of gel thickness, acrylamide/Bis ratio, and polymerization conditions. There is a direct relationship between the electrophoretic mobility and molecular weight of protein standards in the PAU system; however, several proteins including histones H2, H3, H4 and bovine serum albumin have a faster rate of gration than expected. It has been possible to separate and identify the gas vacuole protein from Halobacterium halobium, Halobacterium salinarium strain 5, and the two species of cyanobacteria, Anabaena flos-aquae and Microcystis aeruginosa. Mobility of the gas vacuole proteins in the four species are consistent with molecular weights of 16 800, 16 800, 14 700 and 15 700 respectively. Gels produced using the PAU system can be successfully fluorographed.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150010310
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