Abstract:
:The saline extract of Bauhinia bauhinioides dry seeds was shown to inhibit cruzipain, a cysteine proteinase from Trypanosoma cruzi. The inhibitory activity was assigned to a protein with 164 amino acid residues and molecular mass of 18 034 Da that was purified by chromatography on DEAE-Sephadex, trypsin-Sepharose (removal of trypsin inhibitors), Mono Q and a reversed-phase C4 column. The primary structure is homologous to other plant Kunitz-type inhibitors, but it lacks cysteine residues and therefore the disulfide bridges. No methionine residue was identified by amino acid sequencing. The inhibition of cruzipain fits into a slow-tight binding mechanism with a low dissociation constant (Ki 1.2 nM). The studied Bauhinia protein also inhibits cruzain (Ki 0.3 nM), a C-terminally truncated recombinant species of cruzipain. Cathepsin L, a cysteine proteinase with high homology to cruzipain, is also inhibited (Ki 0.22 nM), but not cathepsin B, papain, bromelain or ficin.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
de Oliveira C,Santana LA,Carmona AK,Cezari MH,Sampaio MU,Sampaio CA,Oliva MLdoi
10.1515/BC.2001.103keywords:
subject
Has Abstractpub_date
2001-05-01 00:00:00pages
847-52issue
5eissn
1431-6730issn
1437-4315journal_volume
382pub_type
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