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Hydrophobic chromatography in the resolution of the interconvertible forms of glycogen phosphorylase
Author(s) -
Er-el Zvi,
Shaltiel Shmuel
Publication year - 1974
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(74)80913-0
Subject(s) - citation , glycogen phosphorylase , library science , chemistry , computer science , glycogen , biochemistry
Homologous series of hydrocarbon-coated agaroses were recently shown to provide a powerful chromatographic tool for the purification of proteins [l-3] . This new technique was named hydrophobic chromatography, as it achieves resolution mainly through differences in the size and distribution of available hydrophobic pockets in the various proteins. Work done in our laboratory and elsewhere [l-l 0] has already demonstrated the wide applicability of this method. One of its advantages lies in the fact that it provides a variety of column families, each constituting a homologous series in which every member has hydrocarbon side chains one-carbon-atom longer than the preceding one. Using exploratory kits of columns [IO] it becomes possible to choose rapidly the most suitable column for a desired purification and to establish optimal conditions for effective retention and subsequent elution of a given protein. This paper illustrates the resolution power of alkyl agaroses (Seph-C,*)l in the separation of the two metabolically interconvertible forms of rabbit muscle glycogen phosphorylase. These two forms are identical in their amino acid sequence, except for a unique serine residue in each of the enzyme protomers (M.W. 100 000 [ 1 l] ) which becomes O-phosphorylated upon conversion of the b form (a dimer) to the a