Papers on
carboxypeptidase B
Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine.Kuranova et al., Moscow, Russia. In Acta Crystallogr Sect F Struct Biol Commun, Oct 2015
Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate.
Laboratory diagnosis of acute pancreatitis: in search of the Holy Grail.Cervellin et al., Parma, Italy. In Crit Rev Clin Lab Sci, 2012
Some interesting biomarkers have been also suggested (e.g., serum and urinary trypsinogen-1, -2 and -3, phospholipase A2, pancreatic elastase, procalcitonin, trypsinogen activated protein, activation peptide of carboxypeptidase B, trypsin-2-alpha1 antitrypsin complex and circulating DNA), but none of them has found widespread application for a variety of reasons, including the inferior diagnostic accuracy when compared with the traditional enzymes, the use of cumbersome techniques, or their recent discovery.
The plasminogen receptor, Plg-R(KT), and macrophage function.Parmer et al., Los Angeles, United States. In J Biomed Biotechnol, 2011
We have used a proteomics approach combining targeted proteolysis with carboxypeptidase B and multidimensional protein identification technology, MudPIT, and a monocyte progenitor cell line to identify a novel transmembrane protein, the plasminogen receptor, Plg-R(KT).
On the discovery of precursor processing.Steiner, Chicago, United States. In Methods Mol Biol, 2010
The subsequent discovery of a similar biosynthetic pathway in yeast led to the identification of eukaryotic families of specialized processing subtilisin-like endopeptidases coupled with carboxypeptidase B-like exopeptidases.
[Role of carboxypeptidase in regulation of fibrinolysis].Kudinov et al., In Ukr Biokhim Zh (1999), 2004
Data are cited about carboxypeptidase B level changes under different physiological conditions and possible methods of fibrinolysis reactions strengthening by means of influence on activity of that carboxypeptidase.