نتایج جستجو برای: aminopeptidase n

تعداد نتایج: 978986  

2009
RAZIEH SABET MOHSEN SHAHLAEI AFSHIN FASSIHI

Quantitative relationships between molecular structure and methionine aminopeptidase-2 inhibitory activity of a series of anthranilic acid sulfonamides derivatives were discovered by different chemometrics tools including FA-MLR, PCRA, GA-PLS. The quality of PCRA equation is better than those derived from FA-MLR. GA-PLS analysis indicated that the topological (IC4 and MPC06), constitutional (nf...

Journal: :Journal of bacteriology 1975
E P Desmond W L Starnes F J Behal

Three enzymes with L- and one enzyme with D-aminopeptidase (EC 3.4.11; alpha-aminoacyl peptide hydrolase) activity have been separated from each other and partially purified from Bacillus subtilis 168 W.T., distinguished with respect to their molecular weights and catalytic properties, and studied in relation to the physiology of this bacterium. One L-aminopeptidase, designated aminopeptidase I...

2017
Muhammad-Al-Mustafa Ismail Laura Mateos Silvia Maioli Paula Merino-Serrais Zeina Ali Maria Lodeiro Eric Westman Eran Leitersdorf Balázs Gulyás Lars Olof-Wahlund Bengt Winblad Irina Savitcheva Ingemar Björkhem Angel Cedazo-Mínguez

Hypercholesterolemia is associated with cognitively deteriorated states. Here, we show that excess 27-hydroxycholesterol (27-OH), a cholesterol metabolite passing from the circulation into the brain, reduced in vivo brain glucose uptake, GLUT4 expression, and spatial memory. Furthermore, patients exhibiting higher 27-OH levels had reduced 18F-fluorodeoxyglucose uptake. This interplay between 27...

Journal: :Journal of immunology 2007
Charles F Towne Ian A York Levi B Watkin John S Lazo Kenneth L Rock

Long oligopeptides (>10 residues) are generated during the catabolism of cellular proteins in the cytosol. To be presented to T cells, such peptides must be trimmed by aminopeptidases to the proper size (typically 8-10 residues) to stably bind to MHC class I molecules. Aminopeptidases also destroy epitopes by trimming them to even shorter lengths. Bleomycin hydrolase (BH) is a cytosolic aminope...

2015
Shalini Iyer Penelope J. La-Borde Karl A.P. Payne Mark R. Parsons Anthony J. Turner R. Elwyn Isaac K. Ravi Acharya

Eukaryotic aminopeptidase P1 (APP1), also known as X-prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are ...

Journal: :The Journal of biological chemistry 2002
Raphael Rozenfeld Xavier Iturrioz Bernard Maigret Catherine Llorens-Cortes

Aminopeptidase A is a zinc metalloenzyme involved in the formation of brain angiotensin III, which exerts a tonic stimulatory action on the central control of blood pressure. Thus, central inhibitors of aminopeptidase A constitute putative central antihypertensive agents. Mutagenic studies have been performed to investigate organization of the aminopeptidase A active site, with a view to design...

2005
Nigel M. HOOPER John HRYSZKO Anthony J. TURNER

Aminopeptidase P (EC 3.4.11.9) was solubilized from pig kidney membranes with bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) and then purified by a combination of anion-exchange and hydrophobic-interaction chromatographies. Contaminating peptidase activities were removed by selective affinity chromatography. The purified enzyme was apparently homogeneous on SDS/PAGE with an Mr...

A. Farhoudi A. M. Abedian Kenari, C. H. Makhdoomi R. M. Nazari

This study was aimed to gain knowledge on the ontogeny of digestive enzymes in common carp larvae at the governmental Warm water Fish Aquaculture Center of Shahid Rajaee in Sari, Mazandaran, Iran. The ontogenetic development of pancreatic (trypsin, chymotrypsin, lipase and α-amylase) and intestinal (alkaline phosphatase and aminopeptidase-N) enzymes were assessed in common carp larvae from firs...

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