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Cross Linking in the Radiolysis of Some Enzymes and Related Proteins

  • K. R. Lynn
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)

Abstract

In non-covalently bound complexes of serveral serine proteases and of ribonuclease with DNA the enzymes were protected against the effects of ionizing radiation. No scavenging by the nucleic acids was observed. Similarly, complexing trypsin with silica protected the enzyme from radiolytic destruction.

Irradiation of solutions of serine proteases required about twice the D37 dose to produce about 10% polymerization: significantly lower relative doses were effective in causing polymerization in both lima bean protease inhibitor and in the octapeptidal hormone oxytocin.

Several sulfhydryl enzymes which have been examined were very efficiently inactivated by ionizing radiation. There was, at the same time, apparent formation of novel intra-molecular-S-S- bonds.

Keywords

Amino Acid Analysis Lima Bean Disulphide Bridge Hydrated Electron Pepsin Digest 
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.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • K. R. Lynn
    • 1
  1. 1.Division of Biological SciencesNational Research Council of CanadaOttawaCanada

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