The uptake of some flavonoids into the vascular endothelium occurs via the bilirubin-specific membrane transporter bilitranslocase. This offers new insights into the vascular effects of both flavonoids and bilirubin.

Health related and environmental side effects associated with conventional chemical coagulants used in water treatment has prompted the search for natural alternatives, especially of plant origin. This study investigated the water coagulation activities of a purified protein from Moringa oleifera seeds on the water from Opa reservoir of Obafemi Awolowo University, Ile-Ife. M. oleifera coagulant protein (MoCP) was purified via ion exchange and gel filtration chromatography respectively. Subunit and native molecular weight as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration was 14.2 kDa and 30.3 kDa respectively. Modified jar test was used to investigate the coagulation activity of the purified protein in comparison to that of conventional chemical coagulant (aluminium sulphate). MoCP significantly reduced turbidity (p < 0.05) and organic load which contributed to about 58.18% reduction in total coliform of treated water. MoCP also elicited promising antimicrobial activity against bacterial isolates in the water from Opa reservoir.

Two forms of rhodanese were purified from the liver of Clarias gariepinus Burchell, designated catfish rhodanese I (cRHD I) and rhodanese II (cRHD II), by ion-exchange chromatography on a CM-Sepharose CL-6B column and gel filtration through a Sephadex G-75 column. The apparent molecular weight obtained for cRHD I and cRHD II was 34,500 +/- 707 and 36,800 +/- 283 Da, respectively. The subunit molecular weight determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis was 33,200 +/- 283 and 35,100 +/- 141 Da for cRHD I and cRHD II, respectively. Atomic absorption spectrophotometric analysis revealed that cRHD II contained a high level of iron (Fe), which presumably was responsible for the brownish colour of the preparation. In contrast, no Fe was identified in cRHD I, and its preparation was colourless. Further characterization of cRHD II gave true Michaelis-Menten constant (K(m)) values of 25.40 +/- 1.70 and 18.60 +/- 1.68 mM for KCN and Na(2)S(2)O(3), respectively, an optimum pH of 6.5 and an optimum temperature of 40 degrees C. The Arrhenius plot of the effects of temperature on the reaction rate consisted of two linear segments with a break occurring at 40 degrees C. The apparent activation energy values from these slopes were 7.3 and 72.9 kcal/mol. Inhibition studies on the cRHD II enzyme showed that the activity of the enzyme was not affected by Mn(2+), Co(2+), Sn(2+), Ni(2+) and NH(4) (+), but Zn(2+) inhibited the enzyme considerably.

A haemagglutinating protein from the saline extracts of Kalanchoe crenata leaves, which agglutinate all human blood types, was purified to homogeneity by ion-exchange chromatography on a DEAE-Cellulose column followed by gel filtration on a Sephadex G-100 column. The purified protein showed one band, both in non-denaturing PAGE and SDS-PAGE. The M r that was determined by SDS-PAGE was 44,000 Da and that estimated from gel filtration was 47,000. Treatment of the haemagglutinating protein with 5 mM EDTA diminished the haemagglutinating activity to 50% of the original level. The addition of divalent cations, 10 mM Mg 2+ , 10 mM Mn 2+ , or 10 mM Ba 2+ , totally restored and enhanced the activity. The protein showed maximum activity over the 3-7 pH range and was heat-resistant. It was also a glycoprotein containing about 1.5% carbohydrate.