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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Aug;78(8):4853–4857. doi: 10.1073/pnas.78.8.4853

Rat alpha-lactalbumin has a 17-residue-long COOH-terminal hydrophobic extension as judged by sequence analysis of the cDNA clones.

A M Dandekar, P K Qasba
PMCID: PMC320273  PMID: 6272279

Abstract

cDNA for rat alpha-lactalbumin has been cloned in bacterial plasmid, and its sequence has been analyzed. The DNA sequence analysis shows that rat alpha-lactalbumin has 17 extra residues beyond the COOH terminus of the alpha-lactalbumin isolated and sequenced to date from other species. The predicted COOH-terminal sequence is hydrophobic and proline rich and bears some resemblance to beta-casein sequences.

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Selected References

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  1. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brew K., Castellino F. J., Vanaman T. C., Hill R. L. The complete amino acid sequence of bovine alpha-lactalbumin. J Biol Chem. 1970 Sep 10;245(17):4570–4582. [PubMed] [Google Scholar]
  3. Brew K., Hill R. L. Lactose biosynthesis. Rev Physiol Biochem Pharmacol. 1975;72:105–158. doi: 10.1007/BFb0031548. [DOI] [PubMed] [Google Scholar]
  4. Brew K., Steinman H. M., Hill R. L. A partial amino acid sequence of -lactalbumin-I of the grey kangaroo (Macropus giganteus). J Biol Chem. 1973 Jul 10;248(13):4739–4742. [PubMed] [Google Scholar]
  5. Brew K. The complete amino-acid sequence of guinea-pig -lactalbumin. Eur J Biochem. 1972 May 23;27(2):341–353. doi: 10.1111/j.1432-1033.1972.tb01844.x. [DOI] [PubMed] [Google Scholar]
  6. Brew K., Vanaman T. C., Hill R. L. Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme. J Biol Chem. 1967 Aug 25;242(16):3747–3749. [PubMed] [Google Scholar]
  7. Brown R. C., Fish W. W., Hudson B. G., Ebner K. E. Isolation and characterization of rat alpha-lactalbumin: a glycoprotein. Biochim Biophys Acta. 1977 Mar 28;491(1):82–92. doi: 10.1016/0005-2795(77)90043-5. [DOI] [PubMed] [Google Scholar]
  8. Chakrabartty P. K., Qasba P. K. Partial purification of rat alpha-lactalbumin mRNA. Nucleic Acids Res. 1977 Jun;4(6):2065–2074. doi: 10.1093/nar/4.6.2065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Enea V., Vovis G. F., Zinder N. D. Genetic studies with heteroduplex DNA of bacteriophage fl. Asymmetric segregation, base correction and implications for the mechanism of genetic recombination. J Mol Biol. 1975 Aug 15;96(3):495–509. doi: 10.1016/0022-2836(75)90175-8. [DOI] [PubMed] [Google Scholar]
  10. Findlay J. B., Brew K. The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65–86. doi: 10.1111/j.1432-1033.1972.tb01812.x. [DOI] [PubMed] [Google Scholar]
  11. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hill R. L., Brew K. Lactose synthetase. Adv Enzymol Relat Areas Mol Biol. 1975;43:411–490. doi: 10.1002/9780470122884.ch5. [DOI] [PubMed] [Google Scholar]
  13. Hopp T. P., Woods K. R. Primary structure of rabbit alpha-lactalbumin. Biochemistry. 1979 Nov 13;18(23):5182–5191. doi: 10.1021/bi00590a024. [DOI] [PubMed] [Google Scholar]
  14. Jung A., Sippel A. E., Grez M., Schütz G. Exons encode functional and structural units of chicken lysozyme. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5759–5763. doi: 10.1073/pnas.77.10.5759. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Katz L., Kingsbury D. T., Helinski D. R. Stimulation by cyclic adenosine monophosphate of plasmid deoxyribonucleic acid replication and catabolite repression of the plasmid deoxyribonucleic acid-protein relaxation complex. J Bacteriol. 1973 May;114(2):577–591. doi: 10.1128/jb.114.2.577-591.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Lingappa V. R., Lingappa J. R., Prasad R., Ebner K. E., Blobel G. Coupled cell-free synthesis, segregation, and core glycosylation of a secretory protein. Proc Natl Acad Sci U S A. 1978 May;75(5):2338–2342. doi: 10.1073/pnas.75.5.2338. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. MacGillivray R. T., Brew K., Barnes K. The amino acid sequence of goat alpha-lactalbumin. Arch Biochem Biophys. 1979 Oct 15;197(2):404–414. doi: 10.1016/0003-9861(79)90262-5. [DOI] [PubMed] [Google Scholar]
  19. Maniatis T., Jeffrey A., van deSande H. Chain length determination of small double- and single-stranded DNA molecules by polyacrylamide gel electrophoresis. Biochemistry. 1975 Aug 26;14(17):3787–3794. doi: 10.1021/bi00688a010. [DOI] [PubMed] [Google Scholar]
  20. Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. McGrogan M., Spector D. J., Goldenberg C. J., Halbert D., Raskas H. J. Purification of specific adenovirus 2 RNAs by preparative hybridization and selective thermal elution. Nucleic Acids Res. 1979 Feb;6(2):593–607. doi: 10.1093/nar/6.2.583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Mercier J. C., Brignon G., Ribadeau-Dumas B. Structure primaire de la caséine kappa B bovine. Séquence complète. Eur J Biochem. 1973 Jun;35(2):222–235. doi: 10.1111/j.1432-1033.1973.tb02829.x. [DOI] [PubMed] [Google Scholar]
  23. Mercier J. C., Gaye P. Study of secretory lactoproteins: primary structures of the signals and enzymatic processing. Ann N Y Acad Sci. 1980;343:232–251. doi: 10.1111/j.1749-6632.1980.tb47255.x. [DOI] [PubMed] [Google Scholar]
  24. Nakhasi H. L., Quasba P. K. Quantitation of milk proteins and their mRNAs in rat mammary gland at various stages of gestation and lactation. J Biol Chem. 1979 Jul 10;254(13):6016–6025. [PubMed] [Google Scholar]
  25. Pelham H. R., Jackson R. J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 1976 Aug 1;67(1):247–256. doi: 10.1111/j.1432-1033.1976.tb10656.x. [DOI] [PubMed] [Google Scholar]
  26. Prasad R., Ebner K. E. Charge forms of Wistar rat alpha-lactalbumin. A contradiction. J Biol Chem. 1980 Jun 25;255(12):5834–5837. [PubMed] [Google Scholar]
  27. Prieels J. P., Bell J. E., Schindler M., Castellino F. J., Hill R. L. Involvement of histidine-32 in the biological activity of alpha-lactalbumin. Biochemistry. 1979 May 1;18(9):1771–1776. doi: 10.1021/bi00576a021. [DOI] [PubMed] [Google Scholar]
  28. Proudfoot N. J., Brownlee G. G. 3' non-coding region sequences in eukaryotic messenger RNA. Nature. 1976 Sep 16;263(5574):211–214. doi: 10.1038/263211a0. [DOI] [PubMed] [Google Scholar]
  29. Qasba P. K., Chakrabartty P. K. Purification and properties of two forms of rat alpha-lactalbumin. J Biol Chem. 1978 Feb 25;253(4):1167–1173. [PubMed] [Google Scholar]
  30. Qasba P. K., Nakhasi H. L. alpha-Lactalbumin mRNA in 4-day lactating rat mammary gland. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4739–4743. doi: 10.1073/pnas.75.10.4739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Ricciardi R. P., Miller J. S., Roberts B. E. Purification and mapping of specific mRNAs by hybridization-selection and cell-free translation. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4927–4931. doi: 10.1073/pnas.76.10.4927. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Richardson R. H., Brew K. Lactose synthase. An investigation of the interaction site of alpha-lactalbumin for galactosyltransferase by differential kinetic labeling. J Biol Chem. 1980 Apr 25;255(8):3377–3385. [PubMed] [Google Scholar]
  33. Roychoudhury R., Jay E., Wu R. Terminal labeling and addition of homopolymer tracts to duplex DNA fragments by terminal deoxynucleotidyl transferase. Nucleic Acids Res. 1976 Jan;3(1):101–116. doi: 10.1093/nar/3.1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Wittek R., Barbosa E., Cooper J. A., Garon C. F., Chan H., Moss B. Inverted terminal repetition in vaccinia virus DNA encodes early mRNAs. Nature. 1980 May 1;285(5759):21–25. doi: 10.1038/285021a0. [DOI] [PubMed] [Google Scholar]

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