This paper reports the preliminary characterization of seed protein fractio
ns from seven varieties of velvet beans (Mucuna pruriens) grown in Nigeria,
using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE
). Three of the most abundant polypeptides, with approximate Mr of 23, 26 a
nd 30 kDa, respectively, were further separated by preparative native-PAGE.
N-terminal sequencing revealed the presence of the consensus sequence DDRE
PV-DT-PL that is also present in the soybean Kunitz-type trypsin inhibitor.
The albumin fraction was also shown to contain both trypsin and chymotryps
in inhibitors through enzyme inhibitor assays. Western analysis using antib
odies, raised against a representative, 23 kDa polypeptide, indicated that
this protein species accumulates exclusively during seed development, sugge
sting a role in seed storage. Haemagglutination assays using rabbit erythro
cytes failed to detect the presence of lectins. The results are discussed w
ithin the context of the role of lectins and protease inhibitors in storage
and plant defence. The findings are also relevant in view of the toxic and
antimetabolic effects of these proteins, which determine the acceptability
and adoption of velvet beans as animal and human feed. (C) 2000 Elsevier S
cience Ltd. All rights reserved.