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-speed swimming ability because of high concentration of Ca2+-binding parvalbumin in fish white muscles. Although parvalbumins are widely studied and conceivably play crucial roles in the physiology and swimming pattern of fishes, still no report is available about their presence in microbes, such as pathogenic fungal species. We detected a DNA sequence in the genome of Trichophyton violaceum and used in silico and polymerase chain reaction (PCR) technique with a designed pair of primers to ...
Fish are the largest and most diverse group of vertebrates. Fish are also a part of the eight food g...
Parvalbumins are low molecular weight, water soluble sarcoplasmic proteins that are found in abundan...
This study aimed to develop a novel approach to determine the correlation between the parvalbumin (P...
Parvalbumins are the most important fish allergens, which are heat-stable, classified in the family ...
Parvalbumins play crucial physiological roles in neuromuscular systems of vertebrates, such as cell-...
Parvalbumins (PVALBs) are low molecular weight calcium-binding proteins. In addition to their role i...
Parvalbumins are proteins that buffer intracellular calcium concentrations and facilitate muscle rel...
Parvalbumin is a calcium-binding muscle protein that is present in all vertebrates. Despite being a ...
The EF-hand calcium binding protein, parvalbumin, is a major fish allergen. Detection of this allerg...
Allergy to bony fish is common and probably increasing world-wide. The major heat-stable pan-fish al...
Parvalbumins are considered as the major allergens of fish. Sturgeons are delivering a number of val...
IgE-mediated allergic reaction to seafood is a common cause of food allergy including anaphylactic r...
Fish parvalbumins are heat-stable calcium-binding proteins that are highly cross-reactive in causing...
Parvalbumin is a calcium-binding muscle protein that is present in all vertebrates. Despite being a ...
Includes abstract.Includes bibliographical references (leaves 101-108).Parvalbumin, the fish major a...
Fish are the largest and most diverse group of vertebrates. Fish are also a part of the eight food g...
Parvalbumins are low molecular weight, water soluble sarcoplasmic proteins that are found in abundan...
This study aimed to develop a novel approach to determine the correlation between the parvalbumin (P...
Parvalbumins are the most important fish allergens, which are heat-stable, classified in the family ...
Parvalbumins play crucial physiological roles in neuromuscular systems of vertebrates, such as cell-...
Parvalbumins (PVALBs) are low molecular weight calcium-binding proteins. In addition to their role i...
Parvalbumins are proteins that buffer intracellular calcium concentrations and facilitate muscle rel...
Parvalbumin is a calcium-binding muscle protein that is present in all vertebrates. Despite being a ...
The EF-hand calcium binding protein, parvalbumin, is a major fish allergen. Detection of this allerg...
Allergy to bony fish is common and probably increasing world-wide. The major heat-stable pan-fish al...
Parvalbumins are considered as the major allergens of fish. Sturgeons are delivering a number of val...
IgE-mediated allergic reaction to seafood is a common cause of food allergy including anaphylactic r...
Fish parvalbumins are heat-stable calcium-binding proteins that are highly cross-reactive in causing...
Parvalbumin is a calcium-binding muscle protein that is present in all vertebrates. Despite being a ...
Includes abstract.Includes bibliographical references (leaves 101-108).Parvalbumin, the fish major a...
Fish are the largest and most diverse group of vertebrates. Fish are also a part of the eight food g...
Parvalbumins are low molecular weight, water soluble sarcoplasmic proteins that are found in abundan...
This study aimed to develop a novel approach to determine the correlation between the parvalbumin (P...