Cathepsins B1 from human fetal membranes.
Cathepsins B1 (EC 3.4.22.1) were isolated from fetal membranes of human placenta, i.e. amnion and chorion-decidua. Purification of the enzymes was achieved by the freezing-thawing technique, ammonium sulphate fractionation and Sephadex gel filtration. Cathepsis B1 separated either from amnion or from chorion-decidua exhibited optimum activity at pH 6.2, and an optimum temperature between 42-45 degrees C. They were inhibited by heavy metals, and compounds which react with the thiol groups. Isoelectric focusing demonstrated three isoenzymes of cathepsin B1 originating from chorion-decidua, while only one band was found for the enzyme from amnion.
D000650:Amnion / Q000201:enzymology*; D002403:Cathepsins / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent; D002823:Chorion / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D005321:Extraembryonic Membranes / Q000201:enzymology*; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007461:Iodoacetates / Q000494:pharmacology; D007700:Kinetics; D008628:Mercury / Q000494:pharmacology; D009928:Organ Specificity; D011247:Pregnancy
D002413:Cations, Divalent; D006902:Hydroxymercuribenzoates; D007461:Iodoacetates; D004492:Edetic Acid; D002403:Cathepsins; D008628:Mercury