ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
A method is reported for analyzing the oligomeric state of proteins in a mixture by multidimensional electrophoresis. Water-soluble proteins prepared from human erythrocyte membranes were separated by means of gel filtration followed by electrophoresis in detergent-free disc gels. The major bands in detergent-free disc gels were identified by means of electrophoresis into a second-dimensional slab gel containing sodium dodecyl sulphate. Detergent-free disc gels were also subjected to two-dimensional electrophoresis into detergent-free slab gels consisting of a continuous gradient of polyacrylamide gel. It was shown that many of the water-soluble proteins existed as distinct oligomers. Spectrin aggregates (tetramer and dimmer) accounted for the slowest moving bands in the detergent-free disc gels. A water-soluble protein of the component 3 region appeared to be present as a hexamer, while component 4.1 was present as a tetramer. Components 4.3, 4.9 and 5 appeared to be present in a large number of aggregated states. Components 7 and 8 formed a heteropolymeric protein complex.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150020408
