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Characterization of a Naturally Occurring Protease Inhibitor in the Hemolymph of the Scorpion, Heterometrus bengalensis

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Title Characterization of a Naturally Occurring Protease Inhibitor in the Hemolymph of the Scorpion, Heterometrus bengalensis
 
Creator Banerjee, Abhijit
Datta, Pradip K
Basu, Pranab S
Datta, Tapash K
 
Subject Infectious Diseases and Immunology
 
Description A protease inhibitor has been purified
by ultracentrifugation, affinity chromatography
on trypsin-sepharose 4B, and chromatofocusing
on PBE-94 from hemolymph of
the scorpion Heterometrus bengalensis. Homogeneity
of the protease inhibitor was demonstrated
by high performance liquid chromatography
(HPLC). The protease inhibitor is a monomeric
glycoprotein with a molecular weight
of 120,000 dalton, which is stable between pH 4
and pH 8. The molecule inhibits serine proteases
like trypsin and ot-chymotrypsin and
shows a noncompetitive mode of inhibition towards
trypsin, with a Ki value of 6.1 x 10 -6
mM. Amino acid analysis shows a preponderance
of aspartic acid, glutamic acid, serine,
and glycine. The protease inhibitor is efficient
in inhibiting phenoloxidase activity in both the
hemolymph and the isolated phenoloxidase.
Melanin synthesis by phenoloxidase may be influenced
by this protease inhibitor.
 
Date 1991
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2290/1/DEVELOPMENTAL_AND_COMPARATIVE_IMMUNOLOGY__V._15_(_4__)213%2D218;1991.pdf
Banerjee, Abhijit and Datta, Pradip K and Basu, Pranab S and Datta, Tapash K (1991) Characterization of a Naturally Occurring Protease Inhibitor in the Hemolymph of the Scorpion, Heterometrus bengalensis. Developmental and Comparative Immunology, 15 (4). pp. 213-218.
 
Relation http://www.eprints.iicb.res.in/2290/