On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. J Biol Chem 1997;272:14477-82.
Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates.
Anisylazoformylarginine: a superior assay substrate for carboxypeptidase B type enzymes.
In the plasma compartment, this family of enzymes is represented by carboxypeptidase N (CPN,  EC 184.108.40.206; also known as lysine carboxypeptidase, kininase I, anaphylatoxin inactivator, or plasma carboxypeptidase B) and the more recently identified carboxypeptidase U (CPU; EC 220.127.116.11; also known as carboxypeptidase R, plasma carboxypeptidase B, or TAFIa).
They cloned the CPU cDNA from human liver and deduced the amino acid sequence of the proenzyme, designating it plasma carboxypeptidase B because the active enzyme very much behaves like pancreatic carboxypeptidase B in terms of enzyme activity (7, 8).
[NH.sub.2]-terminal sequencing reveal the sequence FQSGQV-LAALPRTSRQVQVL, which confirmed its identity as plasma carboxypeptidase B (7).
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.
The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13.
Radioimmunoassay for pancreatic carboxypeptidase B in human serum.