Skip to main content
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.

Full text

PDF
4853

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  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]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES