Cystatins of human placenta.
Two low-molecular protein fractions inhibiting cysteine proteases were isolated from human placenta by alkalization to pH 11, acetone fractionation, affinity chromatography on CM-papain-Sepharose 4B, and Sephadex G-75 gel filtration. The results of polyacrylamide gel electrophoresis, isoelectric focusing indicate that one of there fractions in a dimer of cystatins B, and another is a mixture of cystatins A and B.
Warwas
M
M
Department of Pharmaceutical Biochemistry, Medical Academy, Wrocław, Poland.
Sawicki
G
G
D056655:Cathepsin H; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010206:Papain / Q000037:antagonists & inhibitors; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy; D011480:Protease Inhibitors / Q000302:isolation & purification*
D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D002403:Cathepsins; D003546:Cysteine Endopeptidases; C534126:CTSH protein, human; D056655:Cathepsin H; D010206:Papain