Cysteine proteinase inhibitors in human placenta.
When human placental extract was chromatographed on a Sephadex G-75 column, cysteine proteinase inhibitors with molecular weights of 80 000 and 12 300 were eluted. The high molecular weight peak (CPI-H) was identified as alpha-cysteine proteinase inhibitor. The thermostable low molecular weight peak (CPI-L) inhibited plant proteinases (papain, ficin and bromelain) as well as cathepsins B, H and L isolated from the human placenta. No cross-reactivity was observed between placental CPI-L and serum alpha-CPI.
D000906:Antibodies; D002401:Cathepsin B; D056668:Cathepsin L; D002403:Cathepsins / Q000302:isolation & purification; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors; D004355:Drug Stability; D010450:Endopeptidases; D005260:Female; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010920:Placenta / Q000032:analysis* / Q000201:enzymology; D011247:Pregnancy; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology
D000906:Antibodies; D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D011506:Proteins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; C534281:CTSL protein, human; D056668:Cathepsin L