Results 21 to 30 of about 106,691 (213)

Purification and characterization of arginine deiminase from Klebsiella pneumoniae

open access: yesMedical Journal of Babylon
Background and Objectives: This study was aimed to characterize arginine deiminase (ADI) purified from Klebsiella pneumoniae in vitro. Materials and Methods: Precipitation with 70% saturated ammonium sulphate, ion exchange chromatography with a DEAE ...
Taif Hussien Alameedy   +1 more
doaj   +2 more sources

PEGylation increases antitumoral activity of arginine deiminase of Streptococcus pyogenes. [PDF]

open access: yesAppl Microbiol Biotechnol, 2022
Arginine auxotrophy is a metabolic defect that renders tumor cells vulnerable towards arginine-depleting substances, such as arginine deiminase (ADI) from Streptococcus pyogenes (SpyADI).
Schwarz R   +11 more
europepmc   +2 more sources

Pegylated Arginine Deiminase Depletes Plasma Arginine but Maintains Tissue Arginine Availability in Young Pigs [PDF]

open access: yes, 2021
Pegylated arginine deiminase (ADI-PEG20) results in the depletion of arginine with the production of isomolar amounts of citrulline. This citrulline has the potential to be utilized by the citrulline recycling pathway regenerating arginine and sustaining
Nguyen, Trung C   +9 more
core   +1 more source

The role of the host—Neutrophil biology

open access: yesPeriodontology 2000, EarlyView., 2023
Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple   +4 more
wiley   +1 more source

The bacterial arginine deiminase system (ADI) facilitates the transport and catabolism of L-arginine.

open access: yes, 2022
Bacterial ADIs use the antiporter, ArcD, to import L-arginine and export L-ornithine. Once inside the cell, L-arginine is broken down into L-citrulline by arginine deiminase (ArcA), then to L-ornithine by ornithine transcarbamylase (ArcB).
Tessa C. Herbert (12240029)   +5 more
core   +1 more source

Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the arginine deiminase system of Streptococcus pyogenes [PDF]

open access: yes, 2002
The present study was performed to identify stress-induced putative virulence proteins of Streptococcus suis. For this, protein expression patterns of streptococci grown at 32, 37, and 42°C were compared by one- and two-dimensional gel electrophoresis ...
Gruening, P.   +6 more
core   +1 more source

Screening and Production of Fungal Arginine Degrading Enzymes and Testing Their Effects in Auxotrophic Cancers [PDF]

open access: yesInternational Journal of Medical Arts
The aim of the work: Finding and evaluating fungal arginine-degrading enzymes from various Egyptian soil habitats as anticancer mediators against auxotrophic cancer cells was the goal.
Mohammed Kassab
doaj   +1 more source

LssR plays a positive regulatory role in acid and nisin tolerance response of Lactococcus lactis

open access: yesJournal of Dairy Science, 2022
: In Lactococcus lactis, different regulation mechanisms can be activated to overcome the effects of adverse environmental stresses. Here, a TetR family regulator LssR was demonstrated as a positive regulator in the activation of the mechanisms involved ...
Qianqian Song   +5 more
doaj   +1 more source

A virulence factor as a therapeutic: the probiotic Enterococcus faecium SF68 arginine deiminase inhibits innate immune signaling pathways

open access: yesGut Microbes, 2022
The probiotic bacterial strain Enterococcus faecium SF68 has been shown to alleviate symptoms of intestinal inflammation in human clinical trials and animal feed supplementation studies.
Fereshteh Ghazisaeedi   +8 more
doaj   +1 more source

Bench-to-Bedside Studies of Arginine Deprivation in Cancer

open access: yesMolecules, 2023
Arginine is a semi-essential amino acid which becomes wholly essential in many cancers commonly due to the functional loss of Argininosuccinate Synthetase 1 (ASS1).
George C. Field   +2 more
doaj   +1 more source

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