Results 111 to 120 of about 192,846 (155)

Mechanistic studies on carboxypeptidase A from goat pancreas: Role of arginine residue at the active site

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
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Isolation and purification of cell wall-associated arginine carboxypeptidase fromStreptococcus mitis ATCC 15909

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, Marie-Louise Sund, Helena Lönnies   +2 more
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Carboxypeptidase D Is Up-Regulated in RAW 264.7 Macrophages and Stimulates Nitric Oxide Synthesis by Cells in Arginine-Free Medium

Molecular Pharmacology, 2001
Membrane-bound carboxypeptidase D (CPD) is a B-type carboxypeptidase that specifically cleaves C-terminal Arg or Lys from peptides and proteins. RAW 264.7 cells contained significant membrane-bound CPD activity as shown by activity assays and immunoprecipitation.
V, Hadkar, R A, Skidgel
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Arginine and lysine product inhibition of bovine adrenomedullary carboxypeptidase H, a prohormone processing enzyme

Life Sciences, 1990
Carboxypeptidase H (CPH) is one of the later enzymes in the cascade of proteolytic steps required for the posttranslational processing of peptide hormone precursors, including processing of proenkephalin. In this study, CPH activity in the soluble and membrane fractions of enkephalin-containing bovine chromaffin granules was competitively inhibited by ...
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Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate

Analytical Biochemistry, 2005
Carboxypeptidase U (CPU, TAFIa) is a novel determinant of the fibrinolytic rate. It circulates in blood as an inactive zymogen, procarboxypeptidase U, which is activated during the process of coagulation and fibrinolysis. CPU has a very short half-life at 37 degrees C.
Willemse, Johan, Leurs, Judith, Verkerk, Robert, Hendriks, Dirk   +3 more
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[Enzymatic synthesis of peptides of arginine-chromophore substrates of metalloproteinases and carboxypeptidases].

Bioorganicheskaia khimiia, 1995
Subtilisin 72 sorbed on the surface of macroporous glass catalyzes a condensation of the esters of N-acylated peptides with arginine derivatives in organic solvents. The sorbed enzyme can be used repeatedly, which makes it possible to synthesize the chromophore substrates of metalloproteinases and carbopeptidases of the general formula Dnp-Ala-Ala-Xaa ...
M P, Iusupova, E K, Kotlova, E A, Timokhina, V M, Stepanov   +3 more
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Adult Carboxypeptidase E-Deficient fat/fat Mice Have a Near-Total Depletion of Brain CCK 8 Accompanied by a Massive Accumulation of Glycine and Arginine Extended CCK: Identification of CCK 8 Gly as the Immediate Precursor of CCK 8 in Rodent Brain

Endocrine, 1998
Cholecystokinin (CCK) amide concentrations were reduced over 85% in all the major brain regions of carboxypeptidase E (Cpe)(fat)/Cpe(fat) mice in comparison to control mice. Using an radioimmunoassay (RIA) specific for glycine-extended CCK (CCK Gly), low levels of CCK Gly were detected in control (0.65 ng/g tissue) and were even lower in Cpe(fat)/Cpe ...
W, Wang, B M, Cain, M C, Beinfeld
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Elucidating the effects of arginine and lysine on a monoclonal antibody C-terminal lysine variation in CHO cell cultures

Applied Microbiology and Biotechnology, 2015
Xintao Zhang, Hongping Tang, Yating Sun, Xu-ping Liu, W. Tan, Li Fan   +5 more
semanticscholar   +2 more sources

[A new fluorogenic substrate of carboxypeptidase H--o-coumaroylphenylalanyl-alanyl-arginine].

Bioorganicheskaia khimiia, 1994
New fluorogenic substrate of carboxypeptidase H, Cum-Phe-Ala-Arg-OH, is hydrolyzed by this enzyme to give Cum-Phe-Ala-OH, which is completely extracted by chloroform from the reaction mixture and whose fluorescence increases remarkably by the presence of triethylamine.
V F, Pozdnev, O L, Varlamov, O O, Grigor'ian, O A, Gomazkov   +3 more
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An arginine carboxypeptidase generated during coagulation is diminished or absent in patients with rheumatoid arthritis.

The Journal of laboratory and clinical medicine, 1990
A novel arginine carboxypeptidase that is generated during blood coagulation is diminished in sera obtained from patients with rheumatoid arthritis. The enzyme, which is unrelated to carboxypeptidase N, is more effective than lysine in removing terminal arginine from small synthetic substrates and may function in vivo in the removal of terminal ...
W, Campbell, K, Yonezu, T, Shinohara, H, Okada   +3 more
openaire   +1 more source