Results 11 to 20 of about 2,357 (169)

Fish Processing and Digestion Affect Parvalbumins Detectability in Gilthead Seabream and European Seabass

open access: yesAnimals, 2022
Consumption of aquatic food, including fish, accounts for 17% of animal protein intake. However, fish consumption might also result in several side-effects such as sneezing, swelling and anaphylaxis in sensitized consumers.
Denise Schrama   +7 more
doaj   +1 more source

Identification and characterization of the first fish parvalbumin-like protein data from a pathogenic fungal species, Trichophyton violaceum

open access: yesData in Brief, 2020
Parvalbumins are the most important fish allergens, which are heat-stable, classified in the family of calcium-binding EF-hand proteins, and contain one magnesium binding site. The functional connection between calcium and parvalbumin gives fish the high-
Reza Zolfaghari Emameh   +4 more
doaj   +1 more source

Advanced Proteomic and Bioinformatic Tools for Predictive Analysis of Allergens in Novel Foods

open access: yesBiology, 2023
In recent years, novel food is becoming an emerging trend increasingly more demanding in developed countries. Food proteins from vegetables (pulses, legumes, cereals), fungi, bacteria and insects are being researched to introduce them in meat ...
María López-Pedrouso   +4 more
doaj   +1 more source

Binding of Acrylonitrile to Parvalbumin [PDF]

open access: yesToxicological Sciences, 1996
A previous study has shown that acrylonitrile (ACN) has a long half-life in rainbow trout muscle and that [14C]ACN appears to be bound to a 10,000-Da protein in muscle. The labeled protein was purified from muscle of trout exposed to [14C]ACN, separated on 20% SDS-PAGE, and digested for amino acid analysis and sequence analysis. These studies indicated
J J, Lech   +4 more
openaire   +2 more sources

What Is Parvalbumin for?

open access: yesBiomolecules, 2022
Parvalbumin (PA) is a small, acidic, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily. Structural and physical properties of PA are well studied but recently two highly conserved structural motifs consisting of three amino acids each (clusters I and II), which contribute to the hydrophobic core of the EF-hand domains, have been revealed.
Eugene A. Permyakov, Vladimir N. Uversky
openaire   +4 more sources

Peculiarities of the development, course and diagnostic principles of food anaphylaxis in toddlers

open access: yesZdorovʹe Rebenka, 2021
Food anaphylaxis at an early age can be characterized by a development of nonspecific symptoms, including a child’s persistent crying, drowsiness, tearing of the eyes, sore throat, anxiety, numbness in the limbs, and impaired swallowing and speech. It is
L.V. Besh, O.I. Matsyura
doaj   +1 more source

Engineering parvalbumin for the heart: optimizing the Mg2+ binding properties of rat β-parvalbumin [PDF]

open access: yesFrontiers in Physiology, 2011
Parvalbumin (PV), an EF-hand protein family member, is a delayed calcium buffer that exchanges magnesium for calcium to facilitate fast skeletal muscle relaxation. Genetic approaches that express parvalbumin in the heart also enhance relaxation and show promise of being therapeutic against various cardiac diseases where relaxation is compromised ...
Zhang, Jianchao   +8 more
openaire   +2 more sources

Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin

open access: yesAllergology International, 2004
Background: Parvalbumin is the major and cross-reactive allergen in fish. Sufficient amounts of IgE-reactive recombinant fish parvalbumin are needed for diagnosis and immunotherapy of fish allergy.
Yuki Hamada   +5 more
doaj   +1 more source

Fish allergens at a glance: Variable allergenicity of parvalbumins, the major fish allergens

open access: yesFrontiers in Immunology, 2014
Fish is a common trigger of severe, food-allergic reactions. Only a limited number of proteins induce specific IgE-mediated immune reactions. The major fish allergens are the parvalbumins.
Annette eKuehn   +5 more
doaj   +1 more source

Parvalbumin in rat kidney [PDF]

open access: yesFEBS Letters, 1986
The Ca2+‐binding parvalbumin has been purified for the first time from rat kidney. Its biochemical and immunological properties were indistinguishable from the muscle counterpart. By immunohistochemical methods parvalbumin was localized in part of the distal tubule and proximal collecting duct, similar to the vitamin D‐dependent Ca2+‐binding protein ...
Schneeberger, Peter R.   +1 more
openaire   +2 more sources

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