Abstract
The Murraya Koenigii trypsin inhibitor was found to be the major protein component of the seed extract. The quantity of protein was determined to be approximately 20% of total protein extracted by simple buffer extraction. During different stages of seed development after flowering, the protein concentrations were found to be 5.27, 5.5, 8.5, 18.8 and 20% in 7, 19, 25, 37 and 55 days, respectively. During seed germination, protein degradations were observed from 20% to 12, 7 and 2% in 13, 16 and 22 days, respectively. This inhibitor, earlier purified using ion-exchange and gel filtration chromatography, was purified in single step by affinity column, using Cibacron blue 3GA, with substantial increase in yield. In partial internal sequencing by MALDI-TOF-TOF, six peptides of varying length, totalling 98 amino acid residues, exhibited similarities to the sequences from protease inhibitors, storage proteins and homeodomain-like proteins.
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