scholarly journals A novel system for the two-dimensional electrophoresis of membrane proteins

1977 ◽  
Vol 163 (1) ◽  
pp. 165-168 ◽  
Author(s):  
A G Booth

Membrane proteins were resolved in two dimensions by a novel technique that uses discontinuous electrophoresis in both directions. After electrophoresis in the first direction in chloral hydrate, the membrane proteins were further resolved by a novel system that used organic-base dodecyl sulphates to stack and then resolve them. This latter system has several advantages over conventional electrophoresis in sodium dodecyl sulphate, notably that it avoids the production of artifacts generated by other systems.

Author(s):  
Philip W. Pemberton ◽  
Robert W. Lobley ◽  
Raymond Holmes ◽  
Susanne H. Sørensen ◽  
Kenneth W. Simpson ◽  
...  

Blood ◽  
1979 ◽  
Vol 53 (6) ◽  
pp. 1121-1132 ◽  
Author(s):  
JJ Edwards ◽  
NG Anderson ◽  
SL Nance ◽  
NL Anderson

Abstract Human erythrocyte lysate proteins were resolved into over 250 discrete spots by two-dimensional electrophoresis using isoelectric focusing in the first dimension and electrophoresis in the presence of sodium dodecyl sulfate, (SDS) in the second. The overwhelming excess of hemoglobin has made such analyses difficult in the past. However, with the ISO-DALT two-dimensional electrophoresis system, large numbers of red cell proteins can be mapped in the presence of hemoglobin. When hemoglobin and several other major proteins are removed by adsorption to DEAE-cellulose, additional minor components are seen, giving a total of over 275. With the use of purified preparations, the map positions of five cell enzymes or their subunits were determined: pyruvate kinase, catalase, glucose-6-phosphate dehydrogenase, hypoxanthine phosphoribosyltransferase, and carbonic anhydrase. The mapping techniques described complement and extend those traditionally used to find human red cell protein variants.


1987 ◽  
Vol 33 (4) ◽  
pp. 468-472 ◽  
Author(s):  
T Manabe ◽  
S Visvikis ◽  
M F Dumon ◽  
M Clerc ◽  
G Siest

Abstract We examined lipoproteins and apolipoproteins in serum of a Tangier-disease patient. We used three different techniques of micro-scale two-dimensional electrophoresis: (a) no denaturants; (b) with sodium dodecyl sulfate (SDS) used only in the slab gel electrophoresis; (c) and with urea and a detergent used in isoelectric focusing and with SDS in slab gel electrophoresis. By technique a, an extremely low concentration of high-density lipoproteins (HDL) in the Tangier serum was seen, and lipoproteins that cannot form HDL complexes were detected as multiple spots in the acidic (pl 4 approximately 5) and relatively low apparent molecular mass (20,000 approximately 80,000) region. By technique b, Tangier low-molecular-mass lipoproteins were dissociated into their constituent apolipoproteins, and we observed a higher proportion of apoC-III, together with lower proportions of apoA-I and apoA-II, than in the normal HDL fraction. Technique c showed the total content of apolipoproteins in the whole Tangier serum, as several workers have reported. The presence of low-molecular-mass lipoproteins and a high concentration of apoC-III in this lipoprotein fraction characterized the Tangier serum.


2007 ◽  
Vol 389 (4) ◽  
pp. 1033-1045 ◽  
Author(s):  
Ralf J. Braun ◽  
Norbert Kinkl ◽  
Monika Beer ◽  
Marius Ueffing

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