Abstract
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
Protein & Peptide Letters
Title: A Storage Protein-Like Trypsin Inhibitor from the Moth Bean (Phaseolus acutifolius) with Antiproliferative Activity Toward Lymphoma Cells
Volume: 17 Issue: 6
Author(s): D.Z. Ma, J. Sun, G.Q. Zhang, H.X. Wang and T.B. Ng
Affiliation:
Keywords: antiproliferative, lymphoma cells, moth bean, purification, storage protein, trypsin inhibitor
Abstract: 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.
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Cite this article as:
Ma D.Z., Sun J., Zhang G.Q., Wang H.X. and Ng T.B., A Storage Protein-Like Trypsin Inhibitor from the Moth Bean (Phaseolus acutifolius) with Antiproliferative Activity Toward Lymphoma Cells, Protein & Peptide Letters 2010; 17 (6) . https://dx.doi.org/10.2174/092986610791190408
DOI https://dx.doi.org/10.2174/092986610791190408 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
Call for Papers in Thematic Issues
Therapeutic Proteins and Peptides of Plant Origin
Plants are still the major repository of biologically active substances. In the last two decades, however, natural peptides and proteins of plant origin have gained increasing attention due to their pharmacological activities over a variety of human illness, including those mediated by infections and parasitosis and those involving different cellular ...read more
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