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Journal Article| Volume 253, ISSUE 11, P3907-3912, June 10, 1978

Human plasma carboxypeptidase N. Isolation and characterization.

Open AccessPublished:June 10, 1978DOI:https://doi.org/10.1016/S0021-9258(17)34776-2
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      Human plasma carboxypeptidase N has been purified 2,600-fold from pooled, outdated plasma in a 30% yield.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.

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