PUBLICATION
Purification and Characterization of Parvalbumin Isotypes from Grass Carp (Ctenopharyngodon idella)
- Authors
- Li, Z., You, J., Luo, Y., Wu, J.
- ID
- ZDB-PUB-140621-13
- Date
- 2014
- Source
- Journal of Agricultural and Food Chemistry 62(26): 6212-8 (Journal)
- Registered Authors
- Li, Zheng
- Keywords
- none
- MeSH Terms
-
- Allergens/adverse effects
- Allergens/chemistry
- Allergens/isolation & purification
- Allergens/metabolism
- Amino Acid Sequence
- Animals
- Antibody Specificity
- Carps*
- China
- Dietary Proteins/adverse effects
- Dietary Proteins/chemistry*
- Dietary Proteins/isolation & purification
- Dietary Proteins/metabolism
- Digestion
- Fish Proteins/adverse effects
- Fish Proteins/chemistry*
- Fish Proteins/isolation & purification
- Fish Proteins/metabolism
- Food Hypersensitivity/etiology
- Food Hypersensitivity/metabolism
- Humans
- Models, Biological*
- Molecular Sequence Data
- Molecular Weight
- Parvalbumins/adverse effects
- Parvalbumins/chemistry*
- Parvalbumins/isolation & purification
- Parvalbumins/metabolism
- Protein Isoforms/adverse effects
- Protein Isoforms/chemistry
- Protein Isoforms/isolation & purification
- Protein Isoforms/metabolism
- Rabbits
- Seafood/analysis*
- Seafood/economics
- Sequence Homology, Amino Acid
- PubMed
- 24866418 Full text @ J. Agric. Food Chem.
Citation
Li, Z., You, J., Luo, Y., Wu, J. (2014) Purification and Characterization of Parvalbumin Isotypes from Grass Carp (Ctenopharyngodon idella). Journal of Agricultural and Food Chemistry. 62(26):6212-8.
Abstract
The prevalence of fish allergy is rapidly increasing because of a growing fish consumption driven mainly by a positive image of the fish and health relationship. The purpose of this study was to characterize parvalbumin isotypes from grass carp (Ctenopharyngodon idella), one of the most frequently consumed freshwater fish in China. Three parvalbumin isotypes were purified using consecutive gel filtration and reverse-phase chromatography and denoted as PVI, PVII, and PVIII. The molecular weights of the isotypes were determined to be 11.968, 11.430, and 11.512 kDa, respectively. PVI showed 74% matched amino acids sequence with PV isotype 4a from Danio rerio, while PVII and PVIII showed 46% matched amino acids sequence with PV isotypes from Hypophthalmichthys molitrix. PVII is the dominant allergen, but it was liable to gastrointestinal enzymes as PVIII; however, PVI was resistant to pepsin digestion. A further study is to characterize the epitopes of PVII, the dominant allergen.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping