Results 11 to 20 of about 95,056 (227)

Histidine Decarboxylase in Enterobacteriaceae Revisited [PDF]

open access: yesJournal of Clinical Microbiology, 2004
ABSTRACT With a modification of Taylor's decarboxylation broth, histidine decarboxylase was detected in Enterobacter aerogenes , Morganella morganii , Raoultella ornithinolytica , and some strains of Citrobacter youngae and
Georges, Wauters   +4 more
openaire   +3 more sources

Histidine decarboxylase in experimental tumours

open access: yesJournal of Pharmacy and Pharmacology, 1966
AbstractHistidine decarboxylase activity has been demonstrated in some experimental tumours by direct enzyme assay. The kinetic properties of semi-purified preparations of the histamine-forming enzyme from Rous rat sarcoma and Walker rat mammary carcinoma were similar to those of the “specific” histidine decarboxylase of the foetal rat.
ROLF HÅKANSON
openaire   +3 more sources

Histidine decarboxylase activity in lactic acid bacteria from wine

open access: yesOENO One, 1993
Histidine decarboxylase activity was investigated in 21 strains of lactic acid bacteria isolated from Argentinian wines. This activity is not widely distributed between them, and occurs significatively only in some strains of Lactobacillus hilgardii.
Marta Elena Farías   +3 more
doaj   +2 more sources

Histidine decarboxylase in the stomach of the rat

open access: yesJournal of Pharmacy and Pharmacology, 1967
Abstract Two enzymes capable of decarboxylating l-histidine in vitro have been identified in rat and mouse stomach; one, located in the fundic portion, shows maximal activity at a pH value of 5.6, whilst the other, in the pyloric portion, requires a pH of 7.6 for optimal activity.
A G, Radwan, G B, West
openaire   +3 more sources

Production of biogenic amines by Enterococci

open access: yesCzech Journal of Food Sciences, 2009
Enterococci were presented in all tested samples of raw cow milk (six samples) at the level 103-105 CFU/ml, fresh cheeses (five samples) at the level 102-106 CFU/g and semi-hard cheeses (five samples) at the level 103-105 CFU/g.
Kateřina Kučerová   +4 more
doaj   +1 more source

Structure and mechanism of acetolactate decarboxylase [PDF]

open access: yes, 2013
Acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S ...
Victoria A. Marlow   +9 more
core   +1 more source

Identification and typization of bacteria of the genus Enterococcus supposed to be used for the production of functional foods

open access: yesActa Universitatis Agriculturae et Silviculturae Mendelianae Brunensis, 2007
In this study, the species identification of 12 probiotic strains of the genus Enterococcus from Culture Collection of Dairy Microorganisms Lactoflora (CCDM, Milcom, Tábor, Czech Republic) were done using PCR described by DUTKA-MALEN et al. (1995).
Radka Burdychová
doaj   +1 more source

ClC transporter activity modulates histidine catabolism in Lactobacillus reuteri by altering intracellular pH and membrane potential

open access: yesMicrobial Cell Factories, 2019
Background Histamine is a key mediator of the anti-inflammatory activity conferred by the probiotic organism Lactobacillus reuteri ATCC PTA 6475 in animal models of colitis and colorectal cancer. In L.
Anne E. Hall   +4 more
doaj   +1 more source

Molecular Regulation of Histamine Synthesis

open access: yesFrontiers in Immunology, 2018
Histamine is a critical mediator of IgE/mast cell-mediated anaphylaxis, a neurotransmitter and a regulator of gastric acid secretion. Histamine is a monoamine synthesized from the amino acid histidine through a reaction catalyzed by the enzyme histidine ...
Hua Huang   +6 more
doaj   +1 more source

Cysteine Thioaldehydes: Photolytic Generation, Reactivity, and Biological Implications

open access: yesAngewandte Chemie, EarlyView.
Photolysis of cysteine phenacylsulfides bearing non‐conjugating electron‐withdrawing substituents leads to high conversions into cysteine thioaldehydes through a Norrish type‐II pathway. This methodology enabled the study of the aqueous reactivity of these important biosynthetic intermediates, which, depending on peptide sequence, pH and buffer ...
Ardra Karthika   +9 more
wiley   +2 more sources

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