نتایج جستجو برای: alanine aminopeptidase

تعداد نتایج: 32708  

Journal: :Archives of disease in childhood 1992
H Skopnik R Wallraf B Nies K Tröster G Heimann

Twenty full term neonates with suspected bacterial infection were randomly assigned to a once daily or a twice daily dosage regimen with gentamicin (4 mg/kg/day). Concomitantly all patients were treated with ampicillin (200 mg/kg/day). The gentamicin concentration time curves were analysed by an open two compartment model under steady state conditions on day 4 of treatment. The mean theoretical...

2017
Hassan Mohamed Masoud Mohamed Salah-Eldin Helmy Mohamed Mosaad Abdel-Monsef

Article history: Received on: 03/10/2016 Accepted on: 20/01/2017 Available online: 30/05/2017 Alanine aminopeptidase is purified from camel liver to homogeneity and designated CLAAP. The purification procedure involved anion exchange chromatography on DEAE-cellulose column and gel filtration chromatography on Sephacryl S-300 column. The specific activity of CLAAP is increased to 9.9 folds over ...

2018
Hui-Chuan Chang Camy C-H Kung Tzu-Ting Chang Shu-Chuan Jao Yu-Ting Hsu Wen-Shan Li

Aminopeptidase P, a metalloprotease, targets Xaa-Proline peptides for cleavage [1-4]. There are two forms of human AMPP, a membrane-bound form (hmAMPP) and a soluble cytosolic form (hcAMPP)[5]. Similar to the angiotensin-I-converting enzyme, AMPP plays an important role in the catabolism of inflammatory and vasoactive peptides, known as kinins. The plasma kinin, bradykinin, was used as the subs...

Journal: :The Journal of Cell Biology 1992
D J Klionsky R Cueva D S Yaver

The Saccharomyces cerevisiae APE1 gene product, aminopeptidase I (API), is a soluble hydrolase that has been shown to be localized to the vacuole. API lacks a standard signal sequence and contains an unusual amino-terminal propeptide. We have examined the biosynthesis of API in order to elucidate the mechanism of its delivery to the vacuole. API is synthesized as an inactive precursor that is m...

1997
Edward P. Masler Elena S. Kovaleva

Aminopeptidase was isolated from the plasma fraction of hemolymph from last instar larvae of the gypsy moth Lymantria dispar. Activity was detected using the synthetic substrate L-alanine-4-nitroanilide. Total aminopeptidase activity per microliter of plasma varied with developmental stage. Activity was detected throughout the last (fifth) larval instar and increased throughout the pupal stage....

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1988
S Gomez P Gluschankof A Lepage P Cohen

The somatostatin-28 convertase activity involved in vitro in the processing of somatostatin-28 into the neuropeptides somatostatin-28-(1-12) and somatostatin-14 is composed of an endoprotease and a basic aminopeptidase. We report herein on the purification to apparent homogeneity of these two constituents and on their functional interrelationship. In particular we observed that after various ph...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Lang Chen Yi-Lun Lin Guiqing Peng Fang Li

Mammalian aminopeptidase N (APN) plays multifunctional roles in many physiological processes, including peptide metabolism, cell motility and adhesion, and coronavirus entry. Here we determined crystal structures of porcine APN at 1.85 Å resolution and its complexes with a peptide substrate and a variety of inhibitors. APN is a cell surface-anchored and seahorse-shaped zinc-aminopeptidase that ...

2015
Md Abdul Hye Khan Amit Sharma Kevin R. Rarick Richard J. Roman David R. Harder John D. Imig Johannes Boltze

Cerebral arterial myogenic and autoregulatory responses are impaired in Fawn Hooded hypertensive (FHH) rats. Cerebral autoregulatory responses are restored in the congenic rat strain in which a segment of chromosome 1 from the Brown Norway (BN) rat was transferred into the FHH genetic background (FHH.1BN). The impact of this region on cerebral arterial dilator responses remains unknown. Aminope...

Journal: :Applied and environmental microbiology 1998
J Matos M Nardi H Kumura V Monnet

We sequenced the pepP gene of Lactococcus lactis, which encodes an aminopeptidase P (PepP), and demonstrated that the X-prolyl dipeptidyl aminopeptidase PepX plays a more important role than PepP in nitrogen nutrition. PepP shares homology with methionine aminopeptidases and could play a role in the maturation of nascent proteins.

Journal: :ACS medicinal chemistry letters 2012
Marta Pinto Catherine Rougeot Luis Gracia Mònica Rosa Andrés García Gemma Arsequell Gregorio Valencia Nuria B Centeno

The conformational profiles for the endogenous peptide Opiorphin and a set of seven analogues exhibiting different inhibitory activities toward human aminopeptidase N (hAPN) and human neprilysin (hNEP) were independently computed to deduce a bioactive conformation that Opiorphin may adopt when binding these two enzymes. The conformational space was thoroughly sampled using an iterative simulate...

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