Purification, characterisation and kinetics of a trypsin inhibitor from black gram (Vigna mungo)

✍ Scribed by Vedhachalam Kamalakannan; Venugopal Sathyamoorthy; Dinkar B. Motlag

• Publisher: John Wiley and Sons
• Year: 1984
• Tongue: English
• Weight: 428 KB
• Volume: 35
• Category: Article
• ISSN: 0022-5142
• DOI: 10.1002/jsfa.2740350211

✦ Synopsis

A black gram (Vigna mungo) trypsin inhibitor (BGTI) was purified to homogeneity by ammonium sulphate precipitation, DEAE-cellulose chromatography and affinity chromatography. The homogeneity of the inhibitor was identified by polyacrylamide gel electrophoresis (PAGE), SDS-PAGE, immunodiffusion and immunoelectrophoresis. The isoelectric point of BGTI was 8.32. The molecular weight of the BGTI was found to be about 12500 by both gel filtration and SDS-PAGE. One mole of the BGTI was found to contain 75 amino acid residues, and it was identified as a glycoprotein, comprising about 18.2% carbohydrate. The BGTI was an uncompetitive inhibitor, stable in the pH range 2-10 and in the temperature range 30-80°C for 30 min.