Cross linking in the radiolysis of some enzymes and related proteins.
In non-covalently bound complexes of serveral serine proteases and of ribounclease 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.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D004247:DNA; D004355:Drug Stability; D007202:Indicators and Reagents; D007700:Kinetics; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases / Q000378:metabolism / Q000528:radiation effects*; D011506:Proteins / Q000528:radiation effects*; D012260:Ribonucleases / Q000528:radiation effects*
D000596:Amino Acids; D007202:Indicators and Reagents; D046911:Macromolecular Substances; D010446:Peptide Fragments; D011506:Proteins; D004247:DNA; D012260:Ribonucleases; D010447:Peptide Hydrolases