International Journal of Clinical Nutrition & Dietetics Volume 5 (2019), Article ID 5:IJCND-147, 7 pages
https://doi.org/10.15344/2456-8171/2019/147
https://doi.org/10.15344/2456-8171/2019/147
Research Article
Specific Binding Properties of Mongolian Milk Whey Proteins to Hydrophobic Molecules as Lipocalin
References
- Oe Y, Abe M, Endoh Y, Sakata M, Ichinkhorloo Z, et al. (2014) Phylogenetic analysis of bacteria from Mongolian animal milks and their dairy products by clone library method. Natl Sci Res 28: 31-40.
- Yoshioka N, Kanamoto M, Hamaji Y, Nagai K, Fujimoto D, et al. (2016) Functional analysis for whey protein and peptides in Mongolian animal milks. The 16th Annual Meeting of the Protein Science Society of Japan. The Program and Abstracts 2P-084.
- Vegarud GE, Langsrud T, Svenning C (2000) Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br J Nutr 84: 91-98. View
- Głąb TK, Boratyński J (2017) Potential of Casein as a Carrier for Biologically Active Agents. Top Curr Chem 375: 71. View
- Patel S (2015) Emerging trends in nutraceutical applications of whey protein and its derivatives. J Food Sci Technol 52: 6847-6858. View
- Shimazaki K (2000) Lactoferrin: A marvelous protein in milk? Animal Sci J 71: 329-347. View
- Gifford JL, Hunter HN, Vogel HJ (2005) Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell Mol Life Sci 62: 2588-2598. View
- Sakurai K, Goto Y (2002) Manipulating monomer-dimer equilibrium of bovine Beta-lactoglobulin by amino acid substitution. J Biol Chem 277: 25735-25740. View
- Considine T, Patel HA, Singh H, Creamer LK (2005) Influence of Binding of Sodium Dodecyl Sulfate, All-trans-retinol, Palmitate, and 8-Anilino-1- naphthalenesulfonate on the Heat-Induced Unfolding and Aggregation of α-Lactoglobulin B. J Agric Food Chem 53: 3197-3205. View
- Flower DR, North ACT, Sansom CE (2000) The Lipocalin protein family: structural and sequence overview, Biochim. Biophys Acta 1482: 9-24. View
- George KG, Holt C, Sawyer L (2002) The Ligand-binding Site of Bovine β-Lactoglobulin: Evidence for a Function? J Mol Biol 318: 1043-1055. View
- Busti P, Gatti CA, Delorenzi NJ (1998) Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching. Int J Biol Macromol 23: 143-148. View
- Brew K, Castellino FJ, Vanaman TC, Hill RL (1970) The complete amino acid sequence of bovine α-Lactalbumin. J Biol Chem 245: 4570-4582. View
- Yang Jr. F, Zhang M, Chen J, Liang Y (2006) Structural changes of α-lactalbumin induced by low pH and oleic acid, Biochim. Biophys Acta 1764: 1389-1396. View
- Gustafsson L, Leijonhufvud I, Aronsson A, Mossberg AK, Svanborg C, et al. (2004) Treatment of Skin Papillomas with Topical α-Lactalbumin-Oleic Acid. N Engl J Med 350: 2663-2672. View
- Hakansson A, Zhivotovsky B, Orrenius S, Sabharwal H, Svanborg C, et al. (1995) Apoptosis induced by a human milk protein. Proc Natl Acad Sci USA 92: 8064-8068. View
- Cawthern KM, Narayan M, Chaudhuri D, Permyakov EA, Berliner LJ, et al. (1997) Interactions of α-Lactalbumin with Fatty Acids and Spin Label Analogs. J Biol Chem 272: 30812-30816. View
- Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254. View
- Busti P, Gatti CA, Delorenzi NJ (1998) Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching. Int J Biol Macromol 23: 143-148. View
- Muresan S, Bent A, Wolf FA (2001) Interaction of β-Lactoglobulin with Small Hydrophobic Ligands As Monitored by Fluorometry and Equilibrium Dialysis: Nonlinear Quenching Effects Related to Protein-Protein Association. J Agric Food Chem 49: 2609-2618. View
- Campanacci V, Krieger J, Bette S, Sturgis JN, Lartigue A, et al. (2001) Revisiting the Specificity of Mamestra brassicae and Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay. J Biol Chem 276: 20078-20084. View
- Campanaccia V, Bishopb RE, Blangya S, Tegonia M, Cambillau C, et al. (2006) The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids. FEBS Lett 580: 4877-4883. View
- Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ (2002) Relaxation of β-Structure in Tear Lipocalin and Enhancement of Retinoid Binding. Invest Ophthalmol Vis Sci 43: 3165-3173. View
- Suire S, Stewart F, Beauchamp J, Kennedy MW (2001) Uterocalin, a lipocalin provisioning the preattachment equine conceptus: fatty acid and retinol binding properties, and structural characterization. Biochem J 356: 369-376. View
- Musi V, Spolaore B, Picotti P, Zambonin M, De Filippis V, et al. (2004) Nicked Apomyoglobin: A Noncovalent Complex of Two Polypeptide Fragments Comprising the Entire Protein Chain. Biochemistry 43: 6230-6240. View
- Beg OU, von Bahr-Lindstroem H, Zaidi ZH, Joernvall H (1985) The primary structure of alpha-lactalbumin from camel milk. Eur J Biochem 147: 233- 239. View
- Kaminogawa S, McKenzie HA, Shaw DC (1984) The amino acid sequence of equine alpha-lactalbumin. Biochem Int 9: 539-546. View
- Godovac-Zimmermann J, Shaw D, Conti A, McKenzie HA (1987) Identification and the primary structure of equine alpha-lactalbumin B and C (Equus caballus, Perissodactyla). Biol Chem Hoppe-Seyler 368: 427-433. View
- Jain A, Gour DS, Bisen PS, Prashant, Dubey PP, et al. (2009) Single nucleotide polymorphism (SNP) in alpha-lactalbumin gene of Indian Jamunapari breed of Capra hircus, Small Rumin. Res 82: 156-160. View
- Viaene A, Volckaert G, Joniau M, De Baetselier A, Van Cauwelaert F, et al. (1991) Efficient expression of bovine alpha-lactalbumin in Saccharomyces cerevisiae. Eur J Biochem 202: 471-477. View
- Conti A, Godovac-Zimmermann J, Liberatori J, Braunitzer G (1984) The primary structure of monomeric beta-lactoglobulin I from horse colostrum (Equus caballus, Perissodactyla). Hoppe-Seyler's Z Physiol Chem 365: 1393- 1401. View
- Halliday JA, Bell K, Shaw DC (1991) The complete amino acid sequence of feline beta-lactoglobulin II and a partial revision of the equine betalactoglobulin II sequence. Biochim Biophys Acta 1077: 25-30. View
- Folch JM, Coll A, Sanchez A (1993) Cloning and sequencing of the cDNA encoding goat beta-lactoglobulin. J Anim Sci 71: 2832-2832. View
- Folch J, Coll A, Sanchez A (1994) Complete sequence of the caprine betalactoglobulin gene. J Dairy Sci 77: 3493-3497. View
- Preaux G, Braunitzer G, Schrank B, Stangl A (1979) The amino acid sequence of goat beta-lactoglobulin. Hoppe-Seyler's Z Physiol Chem 360: 1595-1604. View
- Godovac-Zimmermann J, Krause I, Buchberger J, Weiss G, Klostermeyer H, et al. (1990) Genetic variants of bovine beta-lactoglobulin. A novel wildtype beta-lactoglobulin W and its primary sequence. Biol Chem Hoppe- Seyler 371: 255-260. View
- Jamieson AC, Vandeyar MA, Kang YC, Kinsella JE, Batt CA, et al. (1987) Cloning and nucleotide sequence of the bovine beta-lactoglobulin gene. Gene 61: 85-90. View