Rapid Assessment of Cerebral Hemodynamics

Kennady, J. C.

doi:10.2172/4059748

Cited by 1 publication

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“…They have been implicated to have various physiological functions such as regulators of proteolytic cascades, safe storage proteins, and defense molecules against plant pests and pathogens (Ryan, 1990). They have also been used as cancer chemopreventive agents (Kennady, 1994). They have been isolated and characterized from a wide variety of plants, most notably from legumes (Laskowski and Kato, 1980;Moosor et al, 1984;Norton, 1991; and references cited therein).…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Proteinase Inhibitor from Field Bean, Dolichos lablab perpureus L.

Devaraj

Manjunatha

1999

J Protein Chem

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A proteinase inhibitor resembling Bowman-Birk family inhibitors has been purified from the seeds of cultivar HA-3 of Dolichos lablab perpureus L. The protein was apparently homogeneous as judged by SDS-PAGE, PAGE, IEF, and immunodiffusion. The inhibitor had 12 mole% 1/2-cystine and a few aromatic amino acids, and lacks tryptophan. Field bean proteinase inhibitor (FBPI) exhibited a pl of 4.3 and an M r of 18,500 Da. CD spectral studies showed random coiled secondary structure. Conformational changes were detected in the FBPI-trypsin/chymotrypsin complexes by difference spectral studies. Apparent K a values of complexes of inhibitor with trypsin and chymotrypsin were 2.1 X 10 7 M -1 and 3.1 X 10 7 M -1 , respectively. The binary and ternary complexes of FBPI with trypsin and chymotrypsin have been isolated indicating 1:1 stoichiometry with independent sites for cognate enzymes. Amino acid modification studies showed lysine and tyrosine at the reactive sites of FBPI for trypsin and chymotrypsin, respectively.

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