The selective blocking of the polymerization reaction of striated muscle actin leading to a derivative suitable for crystallization. Modification of Tyr-53 by 5-diazonium-(1H)tetrazole.
The polymerization reaction of rabbit muscle actin was completely inhibited by reaction of one amino acid side chain per protein monomer with 5-diazonium-(1H)[14C]tetrazole. A tryptic peptide fingerprint showed a single peptide labeled by the reagent. The peptide was isolated and the labeled amino acid identified by amino acid analysis as Tyr-53. This side chain is not accessible to the reagent in F-actin. The modification is compared to similar inhibitions by other reagents.
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D003979:Diazonium Compounds; D005033:Ethylmaleimide; D046911:Macromolecular Substances; D009132:Muscles / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011817:Rabbits; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013777:Tetrazoles; D014357:Trypsin
D000199:Actins; D000596:Amino Acids; D003979:Diazonium Compounds; D046911:Macromolecular Substances; D010446:Peptide Fragments; D013777:Tetrazoles; D014357:Trypsin; D005033:Ethylmaleimide