Results 71 to 80 of about 95,056 (227)

Increase in histidine decarboxylase activity of rat skin following treatment with compound 48/80

open access: yes, 1959
Repeated injections of rats with compound 48/80, a histamine liberator, results in a marked increase in histidine decarboxylase activity of the skin. The increase is roughly proportional to the duration of treatment.
Piroska Bizony   +2 more
core   +1 more source

Time‐Resolved Multi‐Omics Identify Biomarkers of Immediate Reactions to mRNA Vaccination

open access: yesAllergy, EarlyView.
We compared early vaccine‐induced immune and metabolic signatures and downstream immunity after second and booster BNT162b2 doses in participants with sARs, ISSRs, or no reactions. Neutrophil mobilization, antiviral programs, and robust anti‐S‐antibody responses occurred across reaction groups.
Ana Olivera   +14 more
wiley   +1 more source

Penghambatan Enzim L-Histidine Decarboxylase dari Bakteri Pembentuk Histamin Menggunakan Asam Benzoat

open access: yesJurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan, 2008
ABSTRAK Studi tentang penghambatan enzim L-Histidine Decarboxylase (HDC) menggunakan asam benzoat telah dilakukan. Dalam percobaan ini, enzim HDC diproduksi dari isolat A4, yang diidentifikasi sebagai Enterobacter sp.
Endang Sri Heruwati   +2 more
doaj   +1 more source

Basophils in Immunity: Activation Pathways, Roles in Allergy and AllergoOncology and Application of the Basophil Activation Test

open access: yesAllergy, EarlyView.
ABSTRACT Basophils, the least abundant leukocytes, are increasingly recognised as potent immunomodulators. Upon activation, they rapidly release preformed granule‐associated mediators including histamine and lipid mediators such as LTC4, while cytokine production occurs over a longer timescale, contributing to downstream immune responses.
Jitesh Chauhan   +5 more
wiley   +1 more source

Sequencing, characterization, and gene expression analysis of the histidine decarboxylase gene cluster of morganella morganii

open access: yes, 2014
The histidine decarboxylase gene cluster of Morganella morganii DSM30146T was sequenced, and four open reading frames, named hdcT1, hdc, hdcT2, and hisRS were identified.
R. Muñoz   +11 more
core   +1 more source

Caffeylpyruvate hydrolase from the bioluminescent fungus Neonothopanus gardneri is the key recycling enzyme in the fungal bioluminescence pathway

open access: yesThe FEBS Journal, EarlyView.
Caffeic acid is a central metabolite in the fungal bioluminescence pathway. We identified and characterized caffeylpyruvate hydrolase from Neonothopanus gardneri (ngarCPH) and demonstrate its ability to hydrolyze fungal oxyluciferin into caffeic and pyruvic acids, confirming a complete and self‐sustained fungal bioluminescence cycle.
Caio K. Zamuner   +8 more
wiley   +1 more source

Suppression of rabbit kidney histidine decarboxylase activity by endotoxin

open access: yes, 1963
Previous work has shown that bacterial endotoxins activate an inducible form of histidine decarboxylase present in mammalian tissues. The product of this enzyme, induced histamine, has been postulated to have a circulatory function and to oppose the ...
B. W. Zweifach   +2 more
core   +1 more source

HdcB, a novel enzyme catalysing maturation of pyruvoyl-dependent histidine decarboxylase [PDF]

open access: yes, 2011
Pyruvoyl-dependent histidine decarboxylases are produced as proenzymes that mature by cleavage followed by formation of the pyruvoyl prosthetic group.
Lolkema, Juke S.   +7 more
core   +3 more sources

Evaluation and identification of histamine-forming bacteria on fish products of middle Adriatic Sea

open access: yesItalian Journal of Food Safety, 2013
Regulation EU 2073/2005 sets maximum concentration for histamine in fish and products thereof. To meet these criteria, manufacturers have to define performance objectives, such as the maximum allowed prevalence and number/activity of histamine-producing ...
Rocco Mancusi   +6 more
doaj   +1 more source

Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

open access: yesThe FEBS Journal, EarlyView.
During heme biosynthesis in Gram‐positive bacteria, coproheme decarboxylase (ChdC) catalyzes the conversion of four‐propionate substrate coproheme to the two propionate product heme b. Its active site is universally covered by a flexible linking loop. This study identifies an important histidine residue, which stabilizes the loop in a ChdC homolog.
Nikolaus Falb   +4 more
wiley   +1 more source

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