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The
proteolysis of trypsin inhibitors in legume seeds.
Crit Rev Biotechnol 1988;8(3):197-216
Wilson KA.
Department of Biological Sciences, State University of New York, Binghamton.
The seeds of plants often contain large amounts of proteins, which are subjected
to extensive proteolytic processing during seed development and subsequent
germination. One class of legume seed proteins, the Bowman-Birk-type trypsin
inhibitors, has proved especially useful as a subject in studying these events.
Sequence studies of the trypsin inhibitors from a number of legume species
suggest that many of the inhibitors undergo a limited shortening at the amino
terminus during seed development. However, during germination, the inhibitors
appear to function as storage proteins. As such, they are subjected to extensive
proteolysis, ultimately leading to their destruction. This degradative process
has been studied extensively in the mung bean (Vigna radiata [L.] Wilczek).
Proteolysis of the mung bean trypsin inhibitor involves, at least initially, an
ordered sequence of limited proteolytic cleavages. The two proteases involved in
the initial phases of this degradation have been identified and partially
characterized.
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