Alpha-lactalbumin

Chakraborty, S., Ittah, V., Bai, P., Luo, L., Haas, E., and Peng, Z. Y (2001). Structure and dynamics of the alpha-lactalbumin molten globule Fluorescence studies using proteins containing a single tryptophan residue. Biochemistry 40, 7228-7238. 

Troullier, A., Reinstadler, D., Dupont, Y, Naumann, D., and Forge, V. (2000). Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy. Nat. Struct. Biol. 7, 78-86. 

Kobashigawa Y, Sakurai M, Nitta K. Effect of hydrostatic pressure on unfolding of alpha-lactalbumin volumetric equivalence of the molten globule and unfolded state. Protein Sci. 1999 8 2765-2772. 

Bernaola, G., Echechipia, S., Urrutia, I., Fernandez, E., Audicana, M., and Fernandez de Corres, L. (1994). Occupational asthma and rhinoconjunctivitis from inhalation of dried cow s milk caused by sensitization to alpha-lactalbumin. Allergy 49,189-191. 

Pellegrini, A., Thomas, U., Bramaz, N., Hunziker, P., and von, P. R. (1999). Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. Biochim. Biophys. Acta 1426,439-448. 

Knhlman, B., J.A. Boice, W.J. Wn, R. Fairman, and D.P. Raleigh, Calcium binding peptides from alpha-lactalbumin implications for protein folding and stability. Biochemistry, 1997.36(15) 4607-15. 

Ipsen, R., Otte, J., Qvist, K.B. (2001). Molecular self-assembly of partially hydrolysed alpha-lactalbumin resulting in strong gels with a novel microstructure. Journal of Dairy Research, 68, 277-286. 

Red field, C Schulman, B.A., Milhollen, M.A., Kim, P.S., Dobson, C.M. (1999). Alpha-lactalbumin forms compact molten globule in the absence of disulfide bonds. Nature Structural and Molecular Biology, 10, 948-952. 

Rawitch, A. B. and Hwan, R.-Y. 1979. Anilinonaphthalene sulfonate as a probe for the native structure of bovine alpha lactalbumin Absence of binding to the native monomeric protein. Biochim. Biophys. Res. Commun. 91, 1383-1389. 

Another approach to a study of protein (or nucleic acid) structure and sequence is through Entrez. This can be entered via the NCBI home page. Then click on Proteins to obtain a dialogue box where you can type hu man alpha-lactalbumin and then click on Search. You can retrieve about 25 documents for review. Note that you may also enter BLAST through Entrez,... 

L Huillier, P.J., Davis, S.R. and Bellamy, A.R. (1992) Cytoplasmic delivery of ribozymes leads to efficient reduction in alpha-lactalbumin mRNA levels in Cl 271 mouse cells. UMBO. J., 11,4411 1418. 

Bovine alpha-lactalbumin Bovine beta-lactoglobulin A and B BSA... 

Jarvinen, K.M., Chatchatee, R, Bardina, L., Beyer, K., and Sampson, H.A. 2001. IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow s milk allergy. Int Arch Allergy Immunol 126(2) 111—118. 

Havea, P., Singh, H., Creamer, L.K. 2000. Formation of new protein structures in heated mixtures of BSA and alpha-lactalbumin. JAgric Food Chem 48(5) 1548-1556. 

Hakansson, A., Svensson, M., Mossberg, A.K., Sabharwal, H., Linse, S., Lazou, I., Lonnerdal, B., and Svanborg, C. 2000. A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae. Mol Microbiol 35(3) 589-600. 

Livney, Y.D., Verespej, E., and Dalgleish, D.G. 2003. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin. J Agric Food Chem. 51(27) 8098-8106. 

Maynard, F., Jost, R., and Wal, J.M. 1997. Human IgE binding capacity of tryptic peptides from bovine alpha-lactalbumin. Int Arch Allergy Immunol 113(4) 478—488. 

McGuffey, M.K., Epting, K.L., Kelly, R.M., and Foegeding, E.A. 2005. Denaturation and aggregation of three alpha-lactalbumin preparations at neutral pH. J Agric Food Chem 53(8) 3182-3190. 

Permyakov, E.A. and Berliner, LJ. 2000. alpha-Lactalbumin Structure and function. FEBS Lett 473(3) 269-274. 

Permyakov, S.E., Pershikova, I.V., Khokhlova, T.I., Uversky, V.N., and Permyakov, E.A. 2004. No need to be HAMLET or BAMLET to interact with histones Binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids. Biochemistry 43(19) 5575-5582. 

Slangen, C J. and Visser, S. 1999. Use of mass spectrometry to rapidly characterize the heterogeneity of bovine alpha-lactalbumin. J Agric Food Chem 47(11) 4549-4556. 

Veprintsev, D.B., Permyakov, S.E., Permyakov, E.A., Rogov, V.V., Cawthern, K.M., and Berliner, L.J. 1997. Cooperative thermal transitions of bovine and human apo-alpha-lactalbumins Evidence for a new intermediate state. FEBS Lett 412(3) 625—628. 

Hakansson, A., Andreasson, J., Zhivotovsky, B., Karpman, D., Orrenius, S., and Svanborg, C. 1999. Multimeric alpha-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei. Exp. Cell Res. 246, 451-460. 

Levieux, D. and Ollier, A. 1999. Bovine immunoglobulin G, beta-lactoglobuhn, alpha-lactalbumin and serum albumin in colostrum and milk during the early post partum period. J. Dairy Res. 66, 421-430. 

Otani, H. and Mizumoto, G. 1998. Suppressive effect of lysozymes and alpha-lactalbumins on mitogen-induced proliferative responses of mouse lymphocytes. Anim. Sci. Technol. 69, 1029-1039. 

Pihlanto-Leppala, A., Marnila, P., Hubert, L., Rokka, T., Korhonen, H., and Karp, M. 1999. The effect of alpha-lactalbumin and beta-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103. J. Appl. Microbiol. 87, 540-545. 

McLaren, R. D., Prosser, C. G., Grieve, R. C., and Borissenko, M. (1994). The use of caprylic acid for the extraction of the immunoglobulin fraction from egg yolk of chickens immunized with ovine alpha-lactalbumin. /. Immunol. Methods 177, 175-184. 

Several proteins have been studied and reported to form nanotubes to date. However, the only food protein currently known to possess this ability is alpha-lactalbumin (Graveland-Bikker and de Kruif 2006). Alpha-lactalbumin is one of the key components in whey protein with an isoelectric point (pi) of 4—5. In addition, it s the main protein in breast milk (Lonnerdal and Lien 2003). Observed earlier as the micro-structured stiff gel by Ipsen et al. (Ipsen et al. 2001), self-assembly of alpha-lactalbumin into nanotubes is achieved by its incubation with a protease from Bacillus licheniformis (BLP) acting on the Glu-X and Asp-X bonds, in the presence of Ca ... 

Graveland-Bikker, J., and de Kmif, C. (2005). Self-assembly of hydrolysed alpha-lactalbumin... 

Graveland-Bikker, J.F., Fritz, G., Clatter, O., and de Kmif, C.G. (2006a). Growth and stmc-ture of [alpha]-lactalbumin nanotubes. J. Appl. Crystallogr., 39, 180 184. 

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