Results 131 to 140 of about 3,066 (177)
Optimizing low crude protein diet: Evaluating Glycine as a conditionally essential Amino Acid. [PDF]
Poult SciIqbal W +7 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Arginine Carboxypeptidase (CPR) in Human Plasma Determined with Sandwich ELISA
Microbiology and Immunology, 1999AbstractThere are two types of carboxypeptidases present in human blood, carboxypeptidase N (CPN) and arginine carboxypeptidase (CPR). CPR is generated during coagulation from a precursor (proCPR) which can be converted to the active form by trypsin in vitro.
X, Guo +7 more
openaire +2 more sources
Chemical evidence for a functional arginine residue in carboxypeptidase B
Biochemical and Biophysical Research Communications, 1972Modification 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, 1990A 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 +4 more
openaire +2 more sources
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
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
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
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, 1988Abstract 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 +2 more
openaire +1 more source
Current Microbiology, 1994
An arginine carboxypeptidase was isolated from the cell walls ofStreptococcus mitis ATCC 15909 by mutanolysin extraction of the walls. The enzyme was purified 32-fold by gel filtration on Sephacryl S-300, affinity chromatography on Arginine-Sepharose 4B and by rechromatography on Sephacryl S-300.
Lars E. Linder +2 more
openaire +1 more source
An arginine carboxypeptidase was isolated from the cell walls ofStreptococcus mitis ATCC 15909 by mutanolysin extraction of the walls. The enzyme was purified 32-fold by gel filtration on Sephacryl S-300, affinity chromatography on Arginine-Sepharose 4B and by rechromatography on Sephacryl S-300.
Lars E. Linder +2 more
openaire +1 more source
Archives of Biochemistry and Biophysics, 1985
Chemical modification of carboxypeptidase Ag1 from goat pancreas with phenylglyoxal or ninhydrin led to a loss of enzymatic activity. The inactivation by phenylglyoxal in 200 mM N-ethylmorpholine, 200 mM sodium chloride buffer, pH 8.0, or in 300 mM borate buffer, pH 8.0, followed pseudo-first-order kinetics at all concentrations of the modifier.
R D, Dua, K, Gupta
openaire +2 more sources
Chemical modification of carboxypeptidase Ag1 from goat pancreas with phenylglyoxal or ninhydrin led to a loss of enzymatic activity. The inactivation by phenylglyoxal in 200 mM N-ethylmorpholine, 200 mM sodium chloride buffer, pH 8.0, or in 300 mM borate buffer, pH 8.0, followed pseudo-first-order kinetics at all concentrations of the modifier.
R D, Dua, K, Gupta
openaire +2 more sources