Isolation of Purified Allergens (Cod) by Isoelectric Focusing

El‐Sayed, Sanaa T.; K, Aas

doi:10.1159/000230425

Cited by 101 publications

(41 citation statements)

References 5 publications

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“…pi 4.75 is representative for the major allergenic activity of cod [11]. This fraction was found to contain small amounts of monosaccharides.…”

Section: Discussionmentioning

confidence: 99%

“…The carbohydrate components could not be removed from (DS 22) by these methods as shown by gas chromato graphy. However, one of the constituents isolated by the isoelectric focusing [11], Fr. p i 4.85, possessed high allergenic activity albeit containing no carbohydrate.…”

Section: Discussionmentioning

confidence: 99%

“…pi 4.7j was isolated from the white muscle myogen of cod (Gadus call arias) as outlined elsewhere [1,2,11]. A ratio-recording spectrophotometer, Beckman DK.…”

Section: Methodsmentioning

confidence: 99%

“…Fraction pi 9.60 and fraction pi < 3.00 were not investigated as they were separated close to the electrodes of the isoelectric focusing column [11] and were allergenically almost inactive fractions.…”

Section: Uv-absorption Spectramentioning

confidence: 99%

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Partial Characterization of Homogeneous Allergens (Cod)

Elsayed¹,

K²,

Christensen³

1971

Int Arch Allergy Immunol

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“…pi 4.75 is representative for the major allergenic activity of cod [11]. This fraction was found to contain small amounts of monosaccharides.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…pi 4.7j was isolated from the white muscle myogen of cod (Gadus call arias) as outlined elsewhere [1,2,11]. A ratio-recording spectrophotometer, Beckman DK.…”

Section: Methodsmentioning

confidence: 99%

Section: Uv-absorption Spectramentioning

confidence: 99%

See 2 more Smart Citations

Partial Characterization of Homogeneous Allergens (Cod)

Elsayed¹,

K²,

Christensen³

1971

Int Arch Allergy Immunol

Self Cite

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“…Studies of fisb bypersensitivity and codfisb allergens were initiated many years back by Aas and coworkers. Tbese allergens bave been intensively studied botb clinically and immunologically (1,2,13,14), Allergen M is tbe major allergen of codfisb. It belongs to a large group of vertebrate muscle calcium cbelating proteins, namely parvalbjjmins, Tbe' beneficial function of tbese proteins seems to be mediation of tbe concentration of calcium in muscle (12,29,30).…”

Section: Acceptedjor Publication 7 March 1983mentioning

confidence: 99%

Immunochemical Analysis of Cod Fish Allergen M: Locations of the Immunoglobulin Binding Sites as Demonstrated by the Native and Synthetic Peptides

Elsayed

Apold

1983

Allergy

140

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The major allergen of codfish (Allergen M) is a muscle protein belonging to the family of calcium binding parvalbumins. The primary structure ol the molecule was established and the molecular weight was estimated from the sequence data to be 12,328, Allergen M consists of 113 amino acid residues and one residue of glucose, A molecular arrangement of three domains (AB, CD and EF -the latter two bind one Ca2+ ion each) was described for Allergen M, analogous to carp parvalbumin pi 4,25, The suggested strucutre was based on the extensive intramolecular amino acid homologies and the immunocheinical cross-reactivities of the intact molecule and the two major isolated fragments.The immunological structure of Allergen M was studied by: 1, Modification of certain amino acids residues and study of the reactivity of the modified derivatives, 2, Examination of the immunochemical reactivity of a large number of overlapping peptides obtained by limited and selective tryptic hydrolyses, 3, Solid phase peptide synthesis (SPPS) of segments selected in regard to the reactivity of pre-examined native peptides.The immunological reactivity of the derivatives of Allergen M was assigned by: I, Rocket line immunoelectrophoresis and quantitative precipitation using rabbit anti-Allergen M in precipitating antibody-mediated reactions and, 2, RAST/RAST-inhibition and PK test/PKtest inhibition using sera from individuals allergic to codfish in igE-mediated reactions.The modification of Tyr-30 and Arg-75 in isolated and purified peptides indicated that the former was part of a reactive site whereas the latter did not contribute to the activity. Masking of Arg-residue or unchelating the two calcium ions from the native Allergen M, with the resulting perturbation of the tertiary structure, decreased the allergenicity by approximately 25 %.Two major fragments of Allergen M were produced and purified; TM 1 (residues 1-75) comprising domains AB and CD, and TM2 (residues 76-113) covering domain EF, Both were immunologically reactive; TM 1 showing intermediate reactivity between Allergen M and TM2, A high degree of immunological cross reactivity was evident between TM 1 and TM2, The finding was in concert with the high intramolecular amino acid homologies of Allergen M, and suggested that the reactive sites were repetitively distributed along the polypeptide chain.The immunological reactivity of several long-sequence overlapping peptides obtained by limited and selective trypsin hydrolysis of Allergen M was studied. The immunologically reactive sites were accordingly assigned to the following regions of the chain: 1, Residues 33^4 on the junction between the AB and CD domains, 2, Residues 65-74 on the corresponding junction between the CD and EF domains, 3, Residues 88-96 on the calcium binding loop of the EF domain.These results were cross-examined by SPPS of these segments, A synthetic peptide with the sequence 49-64 of Allergen M, located in the calcium binding loop of the CD domain confirmed the immunological reactivity of this region, Peptide...

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Seafood Proteins and Surimi

Park

Reed

2014

Applied Food Protein Chemistry

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Isolation of Purified Allergens (Cod) by Isoelectric Focusing

Cited by 101 publications

References 5 publications

Partial Characterization of Homogeneous Allergens (Cod)

Partial Characterization of Homogeneous Allergens (Cod)

Immunochemical Analysis of Cod Fish Allergen M: Locations of the Immunoglobulin Binding Sites as Demonstrated by the Native and Synthetic Peptides

Seafood Proteins and Surimi

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