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Inhibitory Effect of Heparin Inhibitor on Camel Urine Lactoferrin K. A. Ahmad; M. S. Jada; A. U. Wurochekke
African Multidisciplinary Journal of Sciences and Artificial Intelligence Vol 2 No 3 (2025): African Multidisciplinary Journal of Sciences and Artificial Intelligence
Publisher : Darul Yasin Al Sys

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.58578/amjsai.v2i3.7782

Abstract

Lactoferrin, an iron-binding protein of the transferrin family, is a basic protein known for its interaction with acidic biomolecules, including heparin proteoglycans. These interactions can influence lactoferrin’s biological functions. This study investigates the inhibitory effect of heparin on lactoferrin activity, revealing a dose-dependent inhibition correlating with increased heparin concentration. Kinetic analysis yielded a Vₘₐₓ of 7.01 U/min, Kₘ of 1037.66 µM, and Kₐₜ of 8.73 × 10⁻¹⁸ s⁻¹, reflecting the enzyme’s catalytic efficiency. Inhibition studies showed that heparin acts as a non-competitive inhibitor, with an IC₅₀, Kᵢ, and K???? all equal to 102.06 µM, indicating moderate affinity for lactoferrin. A binding constant (Kᵦ) of 0.0098 µM⁻¹ further supports this moderate binding interaction. These findings suggest that heparin binds to the N-terminal region of lactoferrin, modulating its function through non-competitive inhibition. The study provides insights into the biochemical regulation of lactoferrin and its interaction with glycosaminoglycans, with potential implications for therapeutic applications involving inflammation and host defense mechanisms.
Purification and Characterization of Lactoferrin from Camel Urine K. A. Ahmad; M. S. Jada; A. U. Wurochekke
African Journal of Biochemistry and Molecular Biology Research Vol 2 No 3 (2025): African Journal of Biochemistry and Molecular Biology Research
Publisher : Darul Yasin Al Sys

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.58578/ajbmbr.v2i3.7705

Abstract

This study reports the isolation, purification, characterization, and antimicrobial activity of lactoferrin derived from camel urine. The lactoferrin was purified through a sequential process involving acetone precipitation, dialysis, ion exchange chromatography, and gel filtration. The partially purified protein was then characterized with respect to its molecular weight, pH and temperature optima, metal ion interaction, and thermal stability. The purification process achieved a 3.23-fold increase in purity with a specific activity of 6.33 U/mg protein and an overall yield of 9.74%. The purified lactoferrin exhibited a molecular weight of 75 kDa and demonstrated optimal activity at pH 7.0 and 40 °C in 50 mM sodium phosphate buffer. Among the metal ions tested, Zn²⁺ enhanced lactoferrin activity, while Mg²⁺ and Al³⁺ acted as strong inhibitors. These findings confirm the potential of camel urine as a novel and viable source of bioactive lactoferrin and lay the groundwork for further biotechnological exploration of its therapeutic applications.
In Vitro Antimicrobial Activity of Camel Urine Lactoferrin K. A. Ahmad; M. S. Jada; A. U. Wurochekke
Kwaghe International Journal of Sciences and Technology Vol 2 No 3 (2025): Kwaghe International Journal of Sciences and Technology
Publisher : Darul Yasin Al Sys

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.58578/kijst.v2i3.7706

Abstract

Lactoferrin, an iron-binding glycoprotein found in various bodily fluids, is widely recognized for its broad-spectrum antimicrobial properties. This study evaluates the in vitro antibacterial and antifungal activity of lactoferrin isolated from camel urine against selected microbial strains. The purified lactoferrin demonstrated notable antibacterial efficacy, producing zones of inhibition ranging from 12–19 mm against Staphylococcus aureus, 10–16 mm against Bacillus subtilis, and 13–21 mm against Escherichia coli. Additionally, antifungal activity was observed against Candida albicans, with inhibition zones ranging from 11–18 mm. The antimicrobial mechanisms are attributed to iron sequestration and disruption of microbial cell membranes in bacteria, and inhibition of fungal growth via interference with cell wall synthesis and membrane integrity. These findings underscore the potential of camel urine-derived lactoferrin as a natural antimicrobial agent and contribute to the growing body of research exploring its biochemical and therapeutic properties.