Human placental cathepsin B1. Isolation and some physical properties.
A reproducible procedure for the isolation, from human placenta, of a cathepsin B1 in a homogeneous state, demonstrated by electrophoretic, ultracentrifugal and enzymic criteria, was carried out. The pH optimum was near pH5.5. The placental enzyme catalysed the release of acid-soluble u.v.-dense products from haemoglobin and myoglobin. It was inhibited by heavy metals and several compounds which react with the thiol groups. The optimum temperature was between 37 degrees and 42 degrees C. The molecular weight of the enzyme was calculated to be 24250.
D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002413:Cations, Divalent; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D004789:Enzyme Activation; D005260:Female; D006454:Hemoglobins; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009211:Myoglobin; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D013056:Spectrophotometry, Ultraviolet; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013696:Temperature; D014461:Ultracentrifugation; D014462:Ultrafiltration
D002413:Cations, Divalent; D006454:Hemoglobins; D009211:Myoglobin; D013439:Sulfhydryl Reagents; D002403:Cathepsins