Sun . 20 Jul 2020
TR | RU | UK | KK | BE |

Alpha-lactalbumin

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
OrthologsSpeciesHumanMouseEntrez
Ensembl
UniProt
RefSeq mRNA

NM_002289

NM_010679

RefSeq protein

NP_002280

NP_034809

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

    Evolution

    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]

    References

    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

    alpha-lactalbumin, alpha-lactalbumin (f76) ige, alpha-lactalbumin allergy, alpha-lactalbumin and beta-lactoglobulin, alpha-lactalbumin cancer, alpha-lactalbumin in whey protein, alpha-lactalbumin rich foods, alpha-lactalbumin structure, alpha-lactalbumin supplement, alpha-lactalbumin wikipedia


    Alpha-lactalbumin Information about

    Alpha-lactalbumin


    • user icon

      Alpha-lactalbumin beatiful post thanks!

      29.10.2014


    Alpha-lactalbumin
    Alpha-lactalbumin
    Alpha-lactalbumin viewing the topic.
    Alpha-lactalbumin what, Alpha-lactalbumin who, Alpha-lactalbumin explanation

    There are excerpts from wikipedia on this article and video

    Random Posts

    La Porte, Indiana

    La Porte, Indiana

    La Porte French for "The Door" is a city in LaPorte County, Indiana, United States, of which it is t...
    Fernando Montes de Oca Fencing Hall

    Fernando Montes de Oca Fencing Hall

    The Fernando Montes de Oca Fencing Hall is an indoor sports venue located in the Magdalena Mixhuca S...
    My Everything (The Grace song)

    My Everything (The Grace song)

    "My Everything" was Grace's 3rd single under the SM Entertainment, released on November 6, 2006 Unli...
    Turkish Straits

    Turkish Straits

    The Turkish Straits Turkish: Türk Boğazları are a series of internationally significant waterways in...