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alpha-lactalbumin supplement, alpha-lactalbumin rich foods
4L41, 1A4V, 1B9O, 1CB3, 1HML, 3B0I, 3B0O

IdentifiersAliasesLALBA, entrez:3906, LYZG, lactalbumin alphaExternal IDsOMIM: 149750 MGI: 96742 HomoloGene: 1720 GeneCards: LALBA
Gene location Human
ChrChromosome 12 human[1]
Band12q1311Start48,567,684 bp[1]
End48,570,066 bp[1]
RNA expression pattern
More reference expression data
RefSeq mRNA



RefSeq protein



Location UCSCChr 12: 4857 – 4857 MbChr 15: 9848 – 9848 MbPubMed search[3][4]Wikidata
1 Function
  • 2 Physical properties
  • 3 Evolution
  • 4 References
  • 5 Further reading
  • 6 External links
  • Function

    α-Lactalbumin is a protein that regulates the production of lactose in the milk of almost all mammalian species[8] In primates, alpha-lactalbumin expression is upregulated in response to the hormone prolactin and increases the production of lactose[9]

    α-Lactalbumin forms the regulatory subunit of the lactose synthase LS heterodimer and β-1,4-galactosyltransferase beta4Gal-T1 forms the catalytic component Together, these proteins enable LS to produce lactose by transferring galactose moieties to glucose As a multimer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity A folding variant of human alpha-lactalbumin that may form in acidic environments such as the stomach, called HAMLET, probably induces apoptosis in tumor and immature cells[5] The corresponding folding dynamics of alpha-lactalbumin is thus highly unusual[10]

    When formed into a complex with Gal-T1, a galactosyltransferase, α-lactalbumin, enhances the enzyme's affinity for glucose by about 1000 times, and inhibits the ability to polymerise multiple galactose units This gives rise to a pathway for forming lactose by converting Gal-TI to Lactose synthase

    Physical properties

    The structure of alpha-lactalbumin is well known and is composed of 123 amino acids and 4 disulfide bridges The molecular weight is 14178 Da, and the isoelectric point is between 42 and 45 One of the main structural differences with beta-lactoglobulin is that it does not have any free thiol group that can serve as the starting-point for a covalent aggregation reaction As a result, pure α-lactalbumin will not form gels upon denaturation and acidification


    The sequence comparison of α-lactalbumin shows a strong similarity to that of lysozymes, specifically the Ca2+-binding c-lysozyme[11] So the expected evolutionary history is that gene duplication of the c-lysozyme was followed by mutation[8] This gene predates the last common ancestor of mammals and birds, which probably puts its origin at about 300 Ma[12]


    1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167531 - Ensembl, May 2017
    2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022991 - Ensembl, May 2017
    3. ^ "Human PubMed Reference:" 
    4. ^ "Mouse PubMed Reference:" 
    5. ^ a b "Entrez Gene: LALBA lactalbumin, alpha-" 
    6. ^ Hall L, Davies MS, Craig RK January 1981 "The construction, identification and characterisation of plasmids containing human alpha-lactalbumin cDNA sequences" Nucleic Acids Res 9 1: 65–84 doi:101093/nar/9165 PMC 326669  PMID 6163135 
    7. ^ Hall L, Emery DC, Davies MS, Parker D, Craig RK March 1987 "Organization and sequence of the human alpha-lactalbumin gene" Biochem J 242 3: 735–42 PMC 1147772  PMID 2954544 
    8. ^ a b Qasba PK, Kumar S 1997 "Molecular divergence of lysozymes and alpha-lactalbumin" Crit Rev Biochem Mol Biol 32 4: 255–306 doi:103109/10409239709082574 PMID 9307874 
    9. ^ Kleinberg JL, Todd J, Babitsky G 1983 "Inhibition by estradiol of the lactogenic effect of prolactin in primate mammary tissue: reversal by antiestrogens LY 156758 and tamoxifen" PNAS 80 13: 4144–4148 doi:101073/pnas80134144 PMC 394217  PMID 6575400 
    10. ^ Bu, Z; Cook, J; Callaway, D J E 2001 "Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin" J Mol Biol 312 4: 865–873 doi:101006/jmbi20015006 PMID 11575938 
    11. ^ Acharya KR, Stuart DI, Walker NP, Lewis M, Phillips DC 1989 "Refined structure of baboon alpha-lactalbumin at 17 A resolution Comparison with C-type lysozyme" J Mol Biol 208 1: 99–127 doi:101016/0022-28368990091-0 PMID 2769757 
    12. ^ Prager EM, Wilson AC 1988 "Ancient origin of lactalbumin from lysozyme: analysis of DNA and amino acid sequences" J Mol Evol 27 4: 326–35 doi:101007/BF02101195 PMID 3146643 

    Further reading

    • Heine WE, Klein PD, Reeds PJ 1991 "The importance of alpha-lactalbumin in infant nutrition" J Nutr 121 3: 277–83 PMID 2002399 
    • Permyakov EA, Berliner LJ 2000 "alpha-Lactalbumin: structure and function" FEBS Lett 473 3: 269–74 doi:101016/S0014-57930001546-5 PMID 10818224 
    • Hall L, Emery DC, Davies MS, et al 1987 "Organization and sequence of the human alpha-lactalbumin gene" Biochem J 242 3: 735–42 PMC 1147772  PMID 2954544 
    • Davies MS, West LF, Davis MB, et al 1987 "The gene for human alpha-lactalbumin is assigned to chromosome 12q13" Ann Hum Genet 51 Pt 3: 183–8 doi:101111/j1469-18091987tb00869x PMID 3479943 
    • Findlay JB, Brew K 1972 "The complete amino-acid sequence of human -lactalbumin" Eur J Biochem 27 1: 65–86 doi:101111/j1432-10331972tb01812x PMID 5049057 
    • Hall L, Craig RK, Edbrooke MR, Campbell PN 1982 "Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene" Nucleic Acids Res 10 11: 3503–3515 doi:101093/nar/10113503 PMC 320727  PMID 6285305 
    • Håkansson A, Zhivotovsky B, Orrenius S, et al 1995 "Apoptosis induced by a human milk protein" Proc Natl Acad Sci USA 92 17: 8064–8068 doi:101073/pnas92178064 PMC 41287  PMID 7644538 
    • Stacey A, Schnieke A, Kerr M, et al 1995 "Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene replacement in mice" Proc Natl Acad Sci USA 92 7: 2835–2839 doi:101073/pnas9272835 PMC 42313  PMID 7708733 
    • Fujiwara Y, Miwa M, Takahashi R, et al 1997 "Position-independent and high-level expression of human alpha-lactalbumin in the milk of transgenic rats carrying a 210-kb YAC DNA" Mol Reprod Dev 47 2: 157–63 doi:101002/SICI1098-279519970647:2<157::AID-MRD5>30CO;2-L PMID 9136116 
    • Lindner RA, Kapur A, Carver JA 1997 "The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin" J Biol Chem 272 44: 27722–9 doi:101074/jbc2724427722 PMID 9346914 
    • Giuffrida MG, Cavaletto M, Giunta C, et al 1998 "The unusual amino acid triplet Asn-Ile-Cys is a glycosylation consensus site in human alpha-lactalbumin" J Protein Chem 16 8: 747–53 doi:101023/A:1026359715821 PMID 9365923 
    • Chandra N, Brew K, Acharya KR 1998 "Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin" Biochemistry 37 14: 4767–4772 doi:101021/bi973000t PMID 9537992 
    • Håkansson A, Andréasson J, Zhivotovsky B, et al 1999 "Multimeric alpha-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei" Exp Cell Res 246 2: 451–60 doi:101006/excr19984265 PMID 9925761 
    • Svensson M, Sabharwal H, Håkansson A, et al 1999 "Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells" J Biol Chem 274 10: 6388–6396 doi:101074/jbc274106388 PMID 10037730 
    • Harata K, Abe Y, Muraki M 1999 "Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method" J Mol Biol 287 2: 347–58 doi:101006/jmbi19992598 PMID 10080897 
    • Last AM, Schulman BA, Robinson CV, Redfield C 2001 "Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry" J Mol Biol 311 4: 909–19 doi:101006/jmbi20014911 PMID 11518539 
    • Bai P, Peng Z 2001 "Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme" J Mol Biol 314 2: 321–9 doi:101006/jmbi20015122 PMID 11718563 
    • Andrews P 1970 "Purification of lactose synthetase a protein from human milk and demonstration of its interaction with alpha-lactalbumin" FEBS Letters 9 5: 297–300 doi:101016/0014-57937080382-9 PMID 11947697 

    External links

    • alpha-Lactalbumin at the US National Library of Medicine Medical Subject Headings MeSH
    • Human LALBA genome location and LALBA gene details page in the UCSC Genome Browser

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