  A method is described where the aminoacyl-tRNA synthetase system is used to
create very small devices for quantitative analysis of the amino acids that
occur in proteins. The basis of the method is that each of the 20 synthetases
and/or a tRNA specific for a different amino acid is separated spatially (e.g.
in tiny chambers or on a surface). The reactions catalyzed by all 20
synthetases are monitored in a spatially resolved manner. Each separately
positioned synthetase or tRNA will signal its cognate amino acid. The
synthetase reactions can be monitored using continuous spectroscopic assays.
Alternatively, since elongation factor Tu;GTP (EF-Tu;GTP) specifically binds
all AA-tRNAs, the aminoacylation reactions catalyzed by the synthetases can be
monitored using ligand assays. Microarrays for amino acid analysis are
suggested. Additionally, it is possible that amino acid analysis arrays can be
integrated with aminopeptidase or carboxypeptidase digestions to produce
miniaturized enzymatic sequenators capable of generating either N- or
C-terminal sequence data at femtomole-attomole levels. The possibility of
parallel processing of many samples in an automated manner is discussed.
