PubMed · 7334821
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D Ripoll, E Marchi, J Benegas. 1981-11-07. A new approach to microtubule depolymerization.. https://doi.org/10.1016/0022-5193(81)90056-4
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The potassium channel T1 domain plays an important role in the regulated assembly of subunit proteins. We have examined the assembly properties of the Shaker channel T1 domain to determine if the domain can self-assemble, the number of subunits in a multimer, Ns and the mechanism of assembly. High pressure liquid chromatography (HPLC) size exclusion chromotography (SEC) separates T1 domain proteins into two peaks. By co-assembly assays, these peaks are identified to be a high molecular weight assembled form and a low molecular weight monomeric form. To determine the Ns of the assembled protein peak on HPLC SEC, we first cross-linked the T1 domain proteins and then separated them on HPLC. Four evenly spaced bands co-migrate with the assembled protein peak; thus, the T1 domain assembles to form a tetramer. The absence of separate dimeric and trimeric peaks of assembled T1 domain protein suggests that the tetramer is the stable assembled state, most probably a closed ring structure.
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A method for two-dimensional micro-electrophoresis and charge determination of fluorescence-labeled membrane molecules in lipid layers is presented. Therefore, the labeled molecules are dissolved in a lipid monolayer which acts as a fluid matrix. The essential part of the sample preparation is an aqueous polymer film composed of agarose onto which the layer is transferred by Langmuir-Blodgett technique. The induced force of an applied electric field leads to a drift of the charged fluorescent molecules. The mobility is determined by an analysis of the steady-state bleach profile which is produced by continuous fluorescence micro-photolysis of a rectangular area of the monolayer. Testing a variety of amphiphilic molecules, measurements yielded values of zero, plus or minus one elementary net charge within a margin of error. The experimental set-up described here can be used for lateral separation, enrichment and isoelectric focusing of membrane components.