J. Biol. Chem., Vol. 261, Issue 18, 8224-8229, 06, 1986
Amino acid sequence of cyanogen bromide fragments of potato phosphorylase
K Nakano, Y Tashiro, Y Kikumoto, M Tagaya and T Fukui
Amino acid sequence analysis of the cyanogen bromide peptides of potato
alpha-glucan phosphorylase was undertaken for comparison with rabbit muscle
glycogen phosphorylase and for elucidation of the structural bases for the
differences in the catalytic and regulatory properties between the animal
and plant enzymes. The potato enzyme was carboxymethylated and cleaved with
cyanogen bromide. The 17 distinct fragments produced were isolated by a
combination of gel filtration, sulfopropyl ion exchange chromatography, and
high performance liquid chromatography. The molecular weights of these
fragments are distributed in a range of 300 to 30,000. Fragment CI has a
blocked amino terminus, and has the same amino acid sequence as CII, which
has been assigned as the amino-terminal fragment of potato phosphorylase.
The blocking group was deduced to be an acetyl group from the results of
fast atom bombardment mass spectrometry of an amino-terminal pentapeptide.
This paper describes the sequence determination of all the cyanogen bromide
fragments of potato phosphorylase. The complete structure is presented in
the following paper (Nakano, K., and Fukui, T. (1986) J. Biol. Chem. 261,
8230-8236).
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