| Autor: |
Walden, Paul D., Blindt, Adrian B., Birkett, Christopher R., Cox, Robert A., Gull, Keith |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 11/6/89, Vol. 185 Issue 2, p383-389, 7p |
| Abstrakt: |
The monoclonal antibody 6-11B-1 recognises specifically the acetylated form of α-tubulin. The acetylation event occurs on a unique lysine residue, lysine 40. Using 6-11B-1, acetylated α-tubulin was detected in myxamoebae but not plasmodia of Physarum polycephalum. Following chemical acetylation plasmodial α-tubulin was detected by 6-11B-1. The monoclonal antibody KMP-1 recognises certain Physarum α-tubulin isotypes but only in non-acetylated form. Whilst recognising all the non-acetylated fraction of myxamoebal α-tubulin only a proportion of plasmodial α-tubulin was recognised by KMP-1. Peptides were synthesised corresponding to the acetylation domains (containing lysine 40) of myxamoebal α-tubulin and the inferred acetylation domains of two plasmodial-specific α-tubulin isotypes. The only difference between the peptides was at a single residue corresponding to amino acid 44 in the polypeptide. Tyrosine was present in myxamoebal α-tubulin and glycine was present in the plasmondial specific peptides; the peptides are referred to as Tyr44 and Gly44 peptides respectively. Both peptides in acetylated form blocked 6-11B-1 reactivity towards acetylated myxamoebal α-tubulin. The Tyr44 but not the Gly44 peptide blocked KMP-1 reactivity towards non-acetylated myxamoebal α-tubulin. Tyrosine at position 44 is not found in any other known α-tubulin. Thus a unique antigenic determinant exists in certain Physarum α-tubulin isotypes, close to the acetylation site at lysine 40. This antigenic determinant forms part of the KMP-1 recognition epitope and explains the unique isotype selectivity of this monoclonal antibody. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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