Volume 21, Issue 84 (Sep 2011)
J Mazandaran Univ Med Sci 2011, 21(84): 44-51 |
Back to browse issues page
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Sharbafi R, Moradian F, Rafiei A, Barzegar A. Isolation and Purification of Bovine Lactoferrin. J Mazandaran Univ Med Sci 2011; 21 (84) :44-51
URL: http://jmums.mazums.ac.ir/article-1-668-en.html
URL: http://jmums.mazums.ac.ir/article-1-668-en.html
Abstract: (15441 Views)
Background and purpose: Lactoferrin is a multifunctional protein, which is useful for clinical and commercial applications. Recently it has been shown that ingestion of Lactoferrin has advantages including: immune system modulation, anti-microbial activity and antioxidant in neonates and adults in both animals and humans. The present study has been conducted with the purpose of isolation and optimal purification of Lactoferrin from cow’s milk.
Materials and methods: Bovine colostrum was collected during 72 hours of delivery. First, milk fat was separated. To Ïsolate Lactoferrin from the rest of the milk proteins, the isolation process was conducted in two steps. Çasein was precipitated using ammonium sulfate and in the next step Lactoferrin was isolated using ÇM-Sephadex-Ç50 cation exchange chromatography column with FPLÇ. To identify the isolated protein SDS-PÂGË method was used.
Results: The pure active protein, with a molecular weight of 80 kDa, with concentration of 2.4 mg/ml was obtained. The degree of purification implementing after cation exchange chromatography column was 4 and purification efficiency 90%.
Çonclusion: Çonsidering the increase in the clinical and nutritional applications of Lactoferrin and particularly its immunomodulatory effects, finding an appropriate and efficient purification method is very important. The results of the study show that the above-mentioned method, apart from simplicity and speed, can result in isolation of highly pure Lactoferrin.
Materials and methods: Bovine colostrum was collected during 72 hours of delivery. First, milk fat was separated. To Ïsolate Lactoferrin from the rest of the milk proteins, the isolation process was conducted in two steps. Çasein was precipitated using ammonium sulfate and in the next step Lactoferrin was isolated using ÇM-Sephadex-Ç50 cation exchange chromatography column with FPLÇ. To identify the isolated protein SDS-PÂGË method was used.
Results: The pure active protein, with a molecular weight of 80 kDa, with concentration of 2.4 mg/ml was obtained. The degree of purification implementing after cation exchange chromatography column was 4 and purification efficiency 90%.
Çonclusion: Çonsidering the increase in the clinical and nutritional applications of Lactoferrin and particularly its immunomodulatory effects, finding an appropriate and efficient purification method is very important. The results of the study show that the above-mentioned method, apart from simplicity and speed, can result in isolation of highly pure Lactoferrin.
Type of Study: Research(Original) |
Send email to the article author
| Rights and permissions | |
 |
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
Articles Copyright © The Author(s). Owned by Mazandaran University of Medical Sciences.
Contact Us
Address: Journal Office, Building No. 2, Mazandaran University of Medical Sciences, Moallem Square, Sari.Tel: +98 (011)34484874 Postal code: 48175-866 E-Mail: jmums@mazums.ac.ir Telefax: +98 (011)33262679
