Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2007949 | Peptides | 2006 | 7 Pages |
Abstract
A peptide, with a molecular mass of 7458 Da, was purified from the seeds of white cloud beans (Phaseolus vulgaris cv. ‘white cloud bean’). This peptide was isolated using a simple protocol consisting of affinity chromatography on Affi-gel blue gel and gel filtration on Superdex 75. The peptide had both antifungal and antibacterial activities. It reduced the activity of HIV-1 reverse transcriptase and it also inhibited translation in a cell-free rabbit reticulocyte lysate system. Its antifungal activity was retained after incubation with trypsin but was reduced when the ambient ionic strength was raised. The peptide elicited a mitogenic response from mouse splenocytes but did not stimulate nitric oxide production in mouse macrophages.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Jack Ho Wong, Xiao Qing Zhang, He Xiang Wang, Tzi Bun Ng,