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Showing 1-16 of 16 results for "P9273" within Papers
H Kato et al.
Journal of biochemistry, 87(4), 1127-1132 (1980-04-01)
Kallikrein in human urine was measured using a fluorogenic peptide substrate, proly-phenyl-alanyl-arginine-4-methylcoumaryl-7-amide (Pro-Phe-Arg-MCA). Using 20 microliters of normal urine, kallikrein activity was quantitatively assayed by incubation with a final concentration of 10(-4) M Pro-Phe-Arg-MCA at 37 degrees C for 90
H Wang et al.
Biomedical chromatography : BMC, 10(3), 139-143 (1996-05-01)
A method was developed for the purification of kallikrein from human urine. The procedure consisted of three steps: ultradialysis, diethyl-(2-hydroxypropyl) aminoethyl (QAE) ion exchange radial flow membrane chromatography and affinity chromatography on aprotinin agarose. It is simple and suitable for
Yogesh Bangale et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 17(6), 628-635 (2003-04-01)
The immunoregulatory neuropeptide vasoactive intestinal peptide (VIP) was cleaved by purified IgG from Fas-defective C3H/gld mice, lupus patients, and autoimmune thyroiditis patients. No VIPase activity was detected in IgG from control mice and humans. Kinetic analyses of VIPase IgG preparations
Y Kitamura et al.
Biochimica et biophysica acta, 1387(1-2), 153-164 (1998-09-28)
The culture medium in which prehatching embryos of the frog, Rana pirica, were cultured (hatching medium) solubilized the vitelline coat (VC) of unfertilized eggs and contained molecules reactive to antibodies (anti-UVS.2) against the Xenopus hatching enzyme (HE). The hydrolyzing activity
L Li et al.
Clinical and experimental immunology, 120(2), 261-266 (2000-05-03)
Chemical catalysis, an effector mechanism utilized by fully assembled antibodies, can also be mediated by the isolated antibody subunits. Because trace amounts of free light chains (L chains) are present in IgG preparations, a detailed study was undertaken to identify
K Uchida et al.
Biochimica et biophysica acta, 614(2), 501-510 (1980-08-07)
Kallikrein (EC 3.4.21.8) was purified from rat stomach by column chromatography on p-aminobenzamidine-Sepharose, DEAE-Sephadex A-50 and Sephadex G-150 and by isoelectric focusing, measuring its activities to hydrolyse L-prolyl-L-phenylalanyl-L-arginine-4-methyl-coumaryl-7-amide and to release kinin from heat-treated rat plasma. the purified stomach kallikrein
S Paul et al.
Journal of immunology (Baltimore, Md. : 1950), 159(3), 1530-1536 (1997-08-01)
Polyreactive and thyroglobulin (Tg)-directed proteolytic activities present in the serum IgG of healthy controls and patients with autoimmune disease were studied by electrophoretic separation of 125I-labeled Tg reaction products and spectrofluorometric measurement of Pro-Phe-Arg-methylcoumarinamide cleavage at the Arg-methylcoumarinamide bond. A
Sven Ruf et al.
Journal of medicinal chemistry, 55(17), 7636-7649 (2012-08-07)
Cathepsin A (CatA) is a serine carboxypeptidase distributed between lysosomes, cell membrane, and extracellular space. Several peptide hormones including bradykinin and angiotensin I have been described as substrates. Therefore, the inhibition of CatA has the potential for beneficial effects in
K Matsuura et al.
Applied biochemistry and biotechnology, 83(1-3), 107-113 (2000-05-29)
Polyclonal Immunoglobulin (Ig) G from patients with rheumatoid arthritis (RA) and healthy subjects hydrolyzed carbobenzoxy-Val-Gly-Arg p-nitroanilide and D-Pro-Phe-Arg p-nitroanilide. RA IgG exhibited higher activity against the former substrate, but not the latter. On the other hand, RA IgG showed reduced
E Nedonchelle et al.
Applied biochemistry and biotechnology, 83(1-3), 287-294 (2000-05-29)
Catalytic autoimmune antibodies from the sera of lupus patients were purified using histidyl-aminohexyl-Sepharose gel and compared with the antibodies purified with protein A and protein G affinity chromatography. The IgG preparations from the histidine affinity column had a much higher
M Hirado et al.
Advances in experimental medicine and biology, 156, 469-479 (1983-01-01)
For the simple purification of porcine pancreas kallikrein, various affinity chromatographies using L-prolyl-L-phenylalanyl-L-arginine (Pro-Phe-Arg-OH), tosyl-L-arginine (Tos-Arg-OH) and acetyl-L-phenylalanyl-L-arginine (Ac-Phe-Arg-OH) as ligands were examined. The purification was performed as follows using the extract from acetone powder of porcine pancreas as starting
M Pathak et al.
Journal of thrombosis and haemostasis : JTH, 13(4), 580-591 (2015-01-22)
Coagulation factor XII is a serine protease that is important for kinin generation and blood coagulation, cleaving the substrates plasma kallikrein and FXI. To investigate FXII zymogen activation and substrate recognition by determining the crystal structure of the FXII protease domain.
Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates.
R Lottenberg et al.
Methods in enzymology, 80 Pt C, 341-361 (1981-01-01)
T Morita et al.
Journal of biochemistry, 82(5), 1495-1498 (1977-11-01)
Twenty peptide-4-methylcoumarin amides (MCA) were newly synthesized and tested as possible substrates for alpha-thrombin, factor Xa, kallikreins, urokinase, and plasmin. These fluorogenic peptides contained arginine-MCA as the carboxyl-terminus. Release of 7-amino-4-methylcoumarin was determined fluorometrically. Of these peptides, the following were
Yung Chyung et al.
Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology, 113(4), 460-466 (2014-07-02)
DX-2930 is a human monoclonal antibody inhibitor of plasma kallikrein under investigation for long-term prophylaxis of hereditary angioedema. To assess the safety, tolerability, pharmacokinetics, and pharmacodynamics of DX-2930 in healthy subjects. A single-center, double-blinded study was performed in 32 healthy
Sven Ruf et al.
Journal of medicinal chemistry, 55(17), 7636-7649 (2012-08-07)
Cathepsin A (CatA) is a serine carboxypeptidase distributed between lysosomes, cell membrane, and extracellular space. Several peptide hormones including bradykinin and angiotensin I have been described as substrates. Therefore, the inhibition of CatA has the potential for beneficial effects in
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