Homology of functionally diverse proteins

Journal/Book: J-Mol-Evol 9 (4), 349-361. 1977;

Abstract: Disulphide-rich proteins of widely differing functions were aligned withthe aid of their half-cystinyl residues. This led to the grouping ofribonuclease, phospholipase A, lysozyme, snake venom toxins, bee andscorpion venom peptides, and the plant proteins potatoe carboxypeptidaseinhibitor, ragweed pollen allergen, mistletoe toxins and pineapplesulfhydryl protease inhibitor into one super-family of proteins. Veryfew deletions/insertions were needed to effect alignment andprobabilities were calculated for random occurrence of the matches thatwere found. Author.

Keyword(s): ALLERGENS/AN (analysis)

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