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The Primary Structure of Fragment TM2 of Allergen M from Cod
Author(s) -
ELSAYED S.,
BAHR LINDSTRÖM H,
BENNICH H.
Publication year - 1974
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.1365-3083.1974.tb01303.x
Subject(s) - allergen , protein primary structure , chemistry , fragment (logic) , residue (chemistry) , homology (biology) , peptide sequence , amino acid , biochemistry , stereochemistry , biology , allergy , immunology , gene , computer science , programming language
The amino acid sequence of the COOH‐terminal fragment TM2 of CIK! allergen M has been determined by the dansyl‐Edman procedure The fragment consists of 58 residues (mol.wt. 3,854). and the sequence shows great homology with the sequence of the corresponding fragment of white muscle albumin from carp. hake, and pike. Unique tor the TM2 (and allergen If) from cod is the presence of a tryptophyl residue at position 5 from the COOH‐terminal end.