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The Primary Structure of Allergen M from Cod
Author(s) -
ELSAYED S.,
BENNICH H.
Publication year - 1975
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1975.tb02618.x
Subject(s) - allergen , primary (astronomy) , medicine , immunology , allergy , physics , astronomy
The complete primary structure of allergen M of cod ( Gadus carias L.) is presented. The amino acid sequence of fragment TM1, the NH 2 ‐terminal peptide of allergen M, was elucidated by the dansyl‐Edman method. It consists of 75 amino acids and 1 glucose residue (mol. wt. 8,492). By summation of the sequence data of fragment TM1 and the previously reported fragment TM2, the intact allergen M has 113 residues (mol. wt. 12,328). Fragment TM1 of cod shows less homology (30.6%) with the corresponding fragments of other reported fish species than does fragment TM2 (42.1%); the intact allergen M shows 34.5% homology. The single half cystine of allergen M was shown to be blocked. Gas chromatographic analysis of the reduced and nonreduced allergen M suggested that the glucose is bound to Cys 18 through an S‐glucosidic bond.