Results 101 to 110 of about 192,846 (155)

Basic carboxypeptidases: regulators of peptide hormone activity

Trends in Pharmacological Sciences, 1988
Randal A Skidgel
exaly   +2 more sources

Effect of selank on the main carboxypeptidases in the rat nervous tissue

Journal of Evolutionary Biochemistry and Physiology, 2012
B. V. Solov’ev, M. Gengin, T. N. Sollertinskaya, I. V. Latynova, L. V. Zhigaeva   +4 more
exaly   +3 more sources

Comparative studies on human carboxypeptidases B and N

Archives of Biochemistry and Biophysics, 1979
T H Plummer
exaly   +2 more sources

Removal of Arg141From the α Chain of Human Hemoglobin by Carboxypeptidases N and M

Circulation Research, 1996
Rajko Igic, E G Erdos, Ervin G Erdos
exaly   +2 more sources

Chemical evidence for a functional arginine residue in carboxypeptidase B

Biochemical and Biophysical Research Communications, 1972
Modification of porcine carboxypeptidase B with phenylglyoxal at pH 7.9 results in a marked decrease of the activity toward the peptides hippurylarginine and Z(Ala) 3 and toward the ester hippurylphenyllactate. Analysis of the kinetics of the modified enzyme revealed that only the k cat values have been changed while the Km values are essentially ...
M M, Werber, M, Sokolovsky
openaire   +2 more sources

Purification and characterization of a new arginine carboxypeptidase in human serum

Biochimica et Biophysica Acta (BBA) - General Subjects, 1990
A carboxypeptidase capable of cleaving basic amino acids from synthetic peptide substrates is present in fresh human serum, and not in human heparinized plasma. Its activity is generated during the process of coagulation. Because of its unstability at room temperature and at 37 degrees C, we named it unstable carboxypeptidase (carboxypeptidase U ...
D, Hendriks, W, Wang, S, Scharpé, M P, Lommaert, M, van Sande   +4 more
openaire   +2 more sources

Fluorescence Probes for Imaging Basic Carboxypeptidase Activity in Living Cells with High Intracellular Retention.

Analytical Chemistry, 2021
Basic carboxypeptidases (basic CPs) cleave the C-terminal basic amino acid of peptides, and their activity is upregulated in some types of cancers. Therefore, detecting the activity of basic CPs in living cells would be important not only for studying ...
Hirohisa Iwaki, M. Kamiya, Minoru Kawatani, Ryosuke Kojima, T. Yamasoba, Y. Urano   +5 more
semanticscholar   +1 more source

Inactivation of Bovine Carboxypeptidase A by Specific Modification of Arginine Residues with Phenylglyoxal

The Journal of Biochemistry, 1974
Upon treatment of bovine carboxypeptidase A [EC 3.4.2.1] with phenylglyoxal, an arginine-specific reagent, at pH 8.0 and 25°C, the peptidase activity was lost very rapidly whereas the esterase activity was lost more slowly. The inhibitor, $phenylpropionic acid, showed some protection against loss of the esterase activity but not against loss of the ...
H, Ikenaga, K, Takahashi
openaire   +2 more sources

An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits

Biochemical and Biophysical Research Communications, 1989
An unstable carboxypeptidase N or B like enzyme is generated as a result of coagulation. This enzyme is derived from some plasma component (s) and not from blood cells or platelets. Furthermore, the activity generated is specific for arginine substrates insofar as small synthetic substrates are concerned.
W, Campbell, H, Okada
openaire   +2 more sources

Arginine carboxypeptidase activity in the male reproductive glands of the silkworm, Bombyx mori

Insect Biochemistry, 1988
Abstract A carboxypeptidase that liberates free arginine from peptides split from proteins by the prostatic endopeptidase, initiatorin, and which serves to supply this amino acid in the spermatophore, was found in the male reproductive system of Bombyx mori. It was consistently detected in the glandula (g.) prostatica at the pH optimum 7.8.
Toshiro Aigaki, Minoru Osanai, Hiroko Kasuga   +2 more
openaire   +1 more source