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        Purification and Partial Characterization of a Lectin from the Fresh Leaves of Kalanchoe crenata (Andr.) Haw

        ( Kuku Adenike ),( Oladiran Babalola Eretan ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.2

        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, 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, 10mM 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.

      • Purification and Partial Characterization of a Lectin from the Fresh Leaves of Kalanchoe crenata (Andr.) Haw

        Adenike, Kuku,Eretan, Oladiran Babalola Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.2

        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.

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        Functional Bioactivities of Soluble Seed Proteins from Two Leguminous Seeds

        Taiwo Scholes Adewole,Boluwatife Bolanle Dudu,Johnson Olaleye Oladele,Oyedotun Moses Oyeleke,Adenike Kuku 한국식품영양과학회 2023 Preventive Nutrition and Food Science Vol.28 No.2

        Storage proteins from Sphenostylis stenocarpa and Phaseolus lunatus were fractionated, and their in vitro bioactivitieswere investigated. Albumin, globulin, prolamin, and glutelin constituents of the respective seeds were successivelyfractionated using the modified Osborne method. Phenylmethylsulfonyl fluoride (1 mM) was used as a protease inhibitor. The antioxidant, anti-inflammatory, and acetylcholinesterase-inhibitory activities of the protein fractions were evaluatedusing different appropriate techniques. Globulin was the predominant fraction, with a yield of 43.21±0.01% and 48.19±0.03% for S. stenocarpa and P. lunatus, respectively, whereas prolamin was not detected in both seeds. The protein fractionmarkedly scavenges hydroxyl radicals, nitric oxide radicals, and 2,2-diphenyl-1-picryldydrazyl radicals with concomitanthigh free radical-reducing power. Albumin and globulin fractions elicited the highest acetylcholinesterase-inhibitory potentialof 48.75% and 49.75%, respectively, indicating their great application potential in managing neurodegenerative diseases. In this study, the albumin, globulin, and glutelin fractions of these underutilized legumes showed great analepticbioactivities, which could be utilized as health-promoting dietary supplements/products.

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