Comparison of Hydrophobic and Strongly Hydrophilic Cleavable Crosslinking Reagents in Intermolecular Bond Formation in Aggregates of Proteins or Protein-RNA

  • H. Fasold
  • H. Bäumert
  • G. Fink
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)


Most of the bifunctional reagents in protein chemistry possess a strongly hydrophobic backbone, derived from aliphatic or aromatic hydrocarbons. Even bifunctionals of more than 30 Å in length of this sort form intramolecular bridges preferentially. in recent years, the intermolecular crosslinking of physiological protein aggregates has gained in importance. as shown in the crosslinking of hemoglobin with two sets of hydrophobic and strongly hydrophilic reagents, derived from azo dyes and tartaric acid, respectively, in this case it is not primarily the length of the bifunctional, but the hydrophilic structure that will enhance intermolecular crosslinking. Artificial dimers of native structure may be obtained. for the crosslinking of RNA to protein, we have synthesized a new reagent, 3-(2-bromo- 3-oxobutane-1-sulphonyl)-propionic acid p-nitrophenyl ester. in a two step reaction, it is attached to adenine and cytosine moieties at pH 6 first, and to lysine side chains at pH 7, 5. The reagent has been applied to the poly-A sequence of globin messenger RNA nucleoprotein.


Tartaric Acid Lysine Side Chain Methyl Vinylketone Intermolecular Crosslinking Bifunctional Reagent 
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. 1.
    H.J. Schramm and Th. Dülffer (1977). This volume.Google Scholar
  2. 2.
    F.C. Hartman, and F. Wold, J.Am.Chem.Soc. 88, 3890(1966).CrossRefGoogle Scholar
  3. 3.
    H. Fasold, J. Klappenberger, Ch. Meyer, and H. Remold, Ang. Chem. 83, 875 (1971).CrossRefGoogle Scholar
  4. 4.
    H. Fasold, Biochem.Zschr. 339, 482 (1964).PubMedGoogle Scholar
  5. 5.
    K. Wetz, H. Fasold, and Ch. Meyer, Anal. Biochem. 58, 347 (1974).PubMedCrossRefGoogle Scholar
  6. 6.
    L.C. Lutter, F. Ortanderl, and H. Fasold, FEBS Letters 48, 288 (1974).PubMedCrossRefGoogle Scholar
  7. 7.
    J. Rinke, K. Möller, A. Ross, and R. Brimacombe,10th Int.Congr. of Biochemistry, Hamburg (1976), Abstr. 03-3-115.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • H. Fasold
    • 1
  • H. Bäumert
    • 1
  • G. Fink
    • 1
  1. 1.Institut für BiochemieUniversity of FrankfurtFrankfurt/Main-NiederradGermany

Personalised recommendations