Results 141 to 150 of about 3,066 (177)

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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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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Assays for Arginine/Lysine Carboxypeptidases: Carboxypeptidases H (E; Enkephalin Convertase), M, and N

1991
Publisher Summary This chapter describes assay methods for arginine/lysine carboxypeptidases. The most frequently employed assay for carboxypeptidase H utilizes a fluorescent substrate, either 5-dimethylaminonaphthalene-l-sulfonyl (dansyl; Dns)-Phe-Leu-Arg or Dns-Phe-Ala-Arg.
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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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[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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[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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[Activity of basic arginine- and lysine-residue cleaving carboxypeptidase in rats of various ages].

Biokhimiia (Moscow, Russia), 1997
Activities of basic carboxypeptidases (CP) in rat brain regions and peripheral tissues were determined on postnatal days 0-90. The highest phenylmethylsulfonyl fluoride-inhibited activity was detected immediately after birth; activity decreases on day 10 with subsequent increase on day 20 and decrease on day 90.
A N, Vernigora, N V, Shchetinina, M T, Gengin   +2 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
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[Properties of basic (splitting off arginine and lysine residues) carboxypeptidases and their role in the functioning of biologically active peptides].

Ukrainskii biokhimicheskii zhurnal (1978), 1993
Properties of carboxypeptidases that cleaved arginine and lysine from C-terminus of peptides are considered. Their role in processing, modulation and inactivation of active peptides are discussed. Mechanisms of regulation of carboxypeptidase H activity are considered.
A N, Vernigora, M T, Gengin
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