title: [Acid proteases from chicken liver. Cooperative hydrolysis of proteins (author's transl)].
abstract: Purified preparations of cathepsin D, BANA-hydrolase activity and dipeptidil aminopeptidase I from chicken liver, show a cooperative effect in the protein hydrolysis (acid-denatured haemoglobin and bovine serum albumin and native bovine serum albumin) at pH 5.0. The nature of the protein substrates determines their sensitivity to enzymatic digestion. The action of cathepsin D on proteins, in contrast which the BANA-hydrolase activity, releases polypeptides with high molecular weight, with scant--NH2 groups which can be valued by the ninhydrin method. These peptide fragments can then be further degraded by the protease BANA-hydrolase and the dipeptidil aminopeptidase I which is not active towards intact proteins.
mesh_terms: D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D002645:Chickens; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins; D002403:Cathepsins; D010447:Peptide Hydrolases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
vernacular_title: Proteasas ácidas de hígado de pollo. Hidrólisis cooperativa de proteínas.