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CPN binds to fibrinogen and is present in a fibrin clot prepared from plasma.
carboxypeptidase N regulates the biologic activity of SDF-1alpha by reducing the chemokine-specific activity
This review summarizes the structure, enzymatic properties and function of this enzyme, including insights gained by the recent elucidation of the crystal structure of the CPN catalytic subunit and structural modeling of the non-catalytic 83 kDa subunit.
circulating CPN/CPB and platelets may potentially contribute to regulating the bioactivity of leukocyte chemoattractant chemerin
Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits\; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.
, arginine carboxypeptidase
, carboxypeptidase K
, carboxypeptidase N catalytic chain
, carboxypeptidase N catalytic subunit
, carboxypeptidase N polypeptide 1 50 kD
, carboxypeptidase N small subunit
, kininase I
, lysine carboxypeptidase
, plasma carboxypeptidase B
, serum carboxypeptidase N
, carboxypeptidase N, polypeptide 1, 50kD
, carboxypeptidase N polypeptide 1