Degradation and inactivation of ceruloplasmin and haptoglobin by rat liver lysosomes and some other proteinases.
Lysosomal fraction was isolated from rat liver by density gradient centrifugation after pervious loading of lysosomes in vivo with Triton WR-1339. Tritosome preparations were incubated at 37 degrees C and pH 5 for 24 hr with purified human ceruloplasmin or haptoglobin. After this period approximately 20% of total alpha amino nitrogen was released from ceruloplasmin and over 40% from haptoglobin. This was accompanied by loss of peroxidase activity of haptoglobin (in complex with haemoglobin), while enzymatic activity of ceruloplasmin remained unaltered. Removal of sialic acid by neuraminidase had no effect on digestion of ceruloplasmin by rat liver tritosomes. Both glycoproteins were resistant to horse leucocyte proteinases and pancreatic eleastase but were easily inactivated by trypsin and chymotrypsin.
D000818:Animals; D002570:Ceruloplasmin / Q000378:metabolism*; D002918:Chymotrypsin / Q000378:metabolism; D004791:Enzyme Inhibitors; D006242:Haptoglobins / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology*; D010447:Peptide Hydrolases; D010544:Peroxidases / Q000378:metabolism; D011092:Polyethylene Glycols; D051381:Rats; D014357:Trypsin / Q000378:metabolism
D004791:Enzyme Inhibitors; D006242:Haptoglobins; D011092:Polyethylene Glycols; D010544:Peroxidases; D002570:Ceruloplasmin; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin