carboxypeptidase


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car·box·y·pep·ti·dase

 (kär-bŏk′sē-pĕp′tĭ-dās′, -dāz′)
n.
Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the end that contains a free carboxyl group.
References in periodicals archive ?
Amplification of carboxypeptidase A gene from genomic DNA of rumen fluid : Various reports indicated that carboxypeptidase A is responsible for OTA degradation (Pitout, 1969; Deberghes et al.
Pancreatic islets and acini produce insulin and carboxypeptidase.
The enzyme responsible for OTA degradation was reported to be carboxypeptidase A (Pitout, 1969).
Another such gene is called fat, which encodes for carboxypeptidase E, an enzyme involved in the activation of a number of prohormones, including insulin.
2006) reported that high dietary zinc increased the activity of several enzymes in the pancreatic tissue (amylase, carboxypeptidase, chymotrypsin, trypsin and lipase) and it might reasonably be expected that such an increase would result in improvements in nutrient digestibility.
Carboxypeptidase U (TAFIa) decreases the efficacy of thrombolytic therapy in ischemic stroke patients.
Furthermore, amidation of the C-terminus is not sufficient to suppress any carboxypeptidase activity (28).
1968; Kundu and Manna, 1975), alpha-amylase (Kundu and Das, 1970) and carboxypeptidase (Blinkovshi et al.
We studied the following proteins: a disintegrin and metalloprotease 8 (Adam 8), CA-125, CA 19-9, carboxypeptidase Al (CPAI), carcinoembryonic antigen (CEA), connective tissue growth factor (CTGF), epidermal growth factor receptor (EGFR), epithelial cell adhesion molecule (EpCAM), Her2/neu (ErbB2), galectin-1, insulin-like growth factor 2 (IGF-2), interleukin (IL)-l[alpha], IL-7, mesothelin, macrophage migration inhibitory factor (MIF), osteopontin, secretory leukocyte peptidase inhibitor (SLPI), tumor necrosis factor [alpha] (TNF-[alpha]), vascular endothelial growth factor (VEGF), and chitinase 3-like 1 (YKL-40).
18 g/L bovine carboxypeptidase A (CpA) and incubated the fibrinogen solution overnight at room temperature (9).
20), is that most of these peptides, including the high abundance ones, are generated by a surprisingly small number of proteins, owing to proteolytic digestion of high abundance proteins by common enzymes such as thrombin, plasmin, and complement proteins, followed by aminopeptidase and carboxypeptidase processing.