Cloning Lectin Genes

  • J. B. Murphy
  • M. E. Etzler
Part of the Springer Laboratory book series (SLM)


The use of recombinant DNA technology is proving to be valuable for studies of lectin structure, biosynthesis, and function. At present, the complete primary structures of a number of plant and animal lectins have been deduced from the sequences of their corresponding mRNAs, and several laboratories are proceeding with site-directed mutagenesis studies in an effort to determine the relationship of lectin structure to function (for recent reviews see Etzler 1992; Lotan 1992). A variety of studies with transgenic organisms has been initiated to determine the factors regulating the biosynthesis of lectins and their intracellular targeting, and it is anticipated that future molecular genetic studies may greatly aid in elucidating the elusive function(s) of these molecules.


Lectin Gene Nucleic Acid Probe Complete Primary Structure Synthetic Oligonucleotide Probe Amino Acid Sequence Information 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (1987–89) Current protocols in molecular biology. Vols 1, 2, John Wiley & Sons, New YorkGoogle Scholar
  2. Aviv H, Leder P (1972) Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci USA 69: 1408–1412PubMedCrossRefGoogle Scholar
  3. Etzler ME (1992) Plant lectins: molecular biology, synthesis and function. In: Allen HJ, Kisailus EC (eds) Glycoconjugates: composition, structure and function, Marcel Dekker, Inc., New York, pp 531–539Google Scholar
  4. Feinberg AP, Vogelstein B (1984) A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 137: 266–267PubMedCrossRefGoogle Scholar
  5. Frischauf A-M, Lehrach H, Poustka A, Murray N (1983) Lambda replacement vectors carrying polylinker sequences. J Mol Biol 170: 827–842PubMedCrossRefGoogle Scholar
  6. Jofuku KD, Goldberg RB (1988) Analysis of plant gene structure. In: Shaw CH (ed) Plant molecular biology: a practical approach, IRL Press, Oxford, pp 37–66Google Scholar
  7. Lotan R (1992) β-Galactoside-binding vertebrate lectins: synthesis, molecular biology, function. In: Allen HJ, Kisailus EC (eds) Glycoconjugates: composition, structure and function, Marcel Dekker, Inc., New York, pp 635–671Google Scholar
  8. Maniatis T, Fritsch EF, Sambrook J (1982) Molecular cloning. A laboratory manual, Cold Spring Harbor Laboratory, New YorkGoogle Scholar
  9. Maxam AM, Gilbert W (1980) Sequencing end-labelled DNA with base-specific chemical cleavages. Meth Enzymol 65: 499–560PubMedCrossRefGoogle Scholar
  10. Short JM (1988) X ZAP: a bacteriophage X expression vector with in vivo excision properties. Nucl Acids Res 16: 7583–7600PubMedCrossRefGoogle Scholar
  11. Taylor B, Powell A (1982) Isolation of plant DNA and RNA. Focus 4: 4–6Google Scholar
  12. Young RA, Davis RW (1983) Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci USA 80: 1194–1198PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • J. B. Murphy
  • M. E. Etzler

There are no affiliations available

Personalised recommendations