Human plasma carboxypeptidase N. Isolation and characterization.
Human plasma carboxypeptidase N has been purified 2,600-fold from pooled, outdated plasma in a 30% yield. Isolation was accomplished by chromatography on DEAE-cellulose and on a p-aminobenzoyl-L-arginine-Sepharose 6B affinity column. Carbohydrate accounts for 17% of the weight calculated from its amino acid and carbohydrate composition. The enzyme appears to consist of three subunits of Mr = 83,000, 55,000, and 49,000 and contains a significant amount of bound zinc. Purified enzyme preparations are very sensitive to proteolytic degradation but are stable for at least 3 months at 4 degrees.
D000596:Amino Acids / Q000032:analysis; D002268:Carboxypeptidases / Q000097:blood*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004355:Drug Stability; D005341:Fibrinolysin; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000097:blood* / Q000302:isolation & purification; D008722:Methods; D014357:Trypsin; D015032:Zinc / Q000032:analysis
D000596:Amino Acids; D002268:Carboxypeptidases; D001121:Lysine Carboxypeptidase; D014357:Trypsin; D005341:Fibrinolysin; D015032:Zinc