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A Storage Protein-Like Trypsin Inhibitor from the Moth Bean (Phaseolus acutifolius) with Antiproliferative Activity Toward Lymphoma Cells

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A 26-kDa trypsin inhibitor with an N-terminal sequence resembling storage proteins was purified from moth beans (Phaseolus acutifolius). It dose-dependently inhibited trypsin with an IC50 value of about 0.38 μM. It inhibited [methyl-3H] thymidine incorporation by lymphoma MBL2 cells with an IC50 value of 20 μM.

Keywords: antiproliferative; lymphoma cells; moth bean; purification; storage protein; trypsin inhibitor

Document Type: Research Article


Publication date: 2010-06-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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