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J. Biol. Chem., Vol. 263, Issue 13, 6005-6008, May, 1988
M Moos Jr, NY Nguyen and TY Liu
A method allowing initial sequencing yields of 60-85% to be consistently
obtained from samples prepared by sodium dodecyl sulfate- polyacrylamide
gel electrophoresis and electrophoretic transfer is described in detail.
Conducting electrophoresis at a pH near neutrality is the single most
important of the modifications made to earlier procedures, but
pre-electrophoresis in the presence of glutathione or sodium thioglycolate
and use of Immobilon polyvinylidene difluoride membranes all contribute to
the success of the technique. When tryptophan was the NH2 terminus of a
protein, the phenylthiohydantoin (PTH)-derivative recovered appeared to be
an irreversible oxidation product if pre-electrophoresis was not performed.
Following pre- electrophoresis, the PTH-derivative recovered co-migrated
with that of unmodified tryptophan, and the recovery was higher. Recovery
of methionine as its PTH-derivative was not affected by pre-
electrophoresis suggesting that thioglycolate in the electrophoresis buffer
during sample separation prevented or reversed oxidation of methionine
sulfur but did not protect tryptophan.
Reproducible high yield sequencing of proteins electrophoretically separated and transferred to an inert support
Division of Biochemistry and Biophysics, Food and Drug Administration, Bethesda, Maryland 20892.
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