Proteolytic degradation of hemoglobin-haptoglobin complex by lysosomal enzymes from rat liver.
The catabolic degradation of hemoglobin and of its complex with haptoglobin by lysosomal enzymes from rat liver was studied with special emphasis on the action of cathepsins D and E. The digestion of free hemoglobin can be mainly attributed to the action of cathepsin D [EC 3.4.23.5], while the digestion of the complex in the pH rand 2-3 is due more to the action of cathepsin E than that of cathepsin D. The enzymic activities of both cathepsins were strongly inhibited by pepstatin, and 4M urea inactivated cathepsin E. Measurements of the peroxidase activity and optical rotatory dispersion of the hemoglobin-haptoglobin complex showed that the complex suffered rapid denaturation below pH 2.9.
D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D006242:Haptoglobins / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D010436:Pepstatins / Q000494:pharmacology; D010544:Peroxidases / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats
D006242:Haptoglobins; D006454:Hemoglobins; D010436:Pepstatins; D010544:Peroxidases; D002403:Cathepsins