ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
A simple, rapid sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method is presented for isolating the α, α' and β subunits of rabbit muscle phosphorylase kinase. The SDS-PAGE procedure can yield milligram amounts of α and β from a single preparative gel and also allows isolation of the α' isozyme free of α. Notably the method provides the purified subunits in a form amenable to structural analysis. Edman degradation of α and α' reveal identical NH2-terminal structures. Amino acid analysis of the electrophoretically purified α and β subunits are in good agreement with their deduced primary structures. The amino acid sequence of 488 residues in α and 713 residues in β were determined by gas phase Edman degradation. The data support the recently deduced primary structures of α (Zander et al., Proc. Natl. Acad. Sci. USA 1988, 85, 2929-2933) and of β (Kilimann et al., Proc. Natl. Acad. Sci. USA, 1988, 85, 9381-9385).
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150110206
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