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On
Protease inhibitors
Submitted to:
Dr. Sashi Madaan
Dapartment of Biochemistry
Submitted by:
Punesh
Ph.D. Biochemistry
INTRODUCTION
4. Mustard trypsin inhibitor family: The seeds of cruciferous plants (Cruciferae) contain
thermostable low molecular weight trypsin inhibitors. In the seed of rape (Brassica napus
L.), these inhibitors account for 60–85% of total trypsin-inhibiting activity. The first
inhibitor to be obtained with a high degree of purity (MTI-2) was isolated from the seed
of white mustard (Sinapis alba L.). MTI-2 has a molecular weight of 7 kDa; its molecule
contains 63 amino acids, including eight Cys residues forming four disulfide bonds. An
inhibitor with closely similar properties (RTI) was isolated from the seed of oil rape
(Brassica napus (L.) var. oleifera). MTI-2 and RTI were shown to have homologous
primary structures (70% amino acid residues are shared), which differed from any other
structures of plant inhibitors of serine proteinases known at that time. Subsequent studies
demonstrated the presence of several forms of the inhibitors in rape and mustard seeds
5. Family of trypsin and α-amylase inhibitors from cereal grains: Trypsin inhibitors,
which account for 5−10% of total water-soluble protein in barley, wheat, and rye seeds,
are classified with two different families. The inhibitors of the germ portion of caryopsis
belong to the Baumann–Birk family (described above), whereas the inhibitors contained
in the endosperm constitute a separate family, which embraces the inhibitors of trypsin
and heterologous α-amylases. Trypsin inhibitors of these two types differ in both the
location within the caryopsis and the behavior throughout seed development and
germination
6. Potato inhibitor I family: Chymotrypsin inhibitor I was isolated from potato tubers and
crystallized in 1963. In addition to chymotrypsin, this protein acts on microbial serine
proteinases and inhibits trypsin (even though weakly). The inhibitor has a molecular
weight of 41 kDa; it is an oligomer composed of five structurally similar protomers.
7. Potato inhibitor II family: The first representatives of this family were isolated from
potato tubers and tomato leaves. These proteins act as potent inhibitors of chymotrypsin
and subtilisin, their effects on trypsin being less pronounced. The molecular weight of
each inhibitor approximates 21 kDa; the molecules are dimers of similar but not
completely identical subunits.