Protein synthesis in rabbit reticulocytes. Preparation of homogeneous Met-tRNAf deacylase and studies of its role in protein synthesis.
Met-tRNAf deacylase from reticulocyte ribosomes has been purified to homogeneity. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the homogeneous preparation gives a single protein band corresponding to a molecular weight of approximately 67,000. Purified Met-tRNAf deacylase degrades free Met-tRNAf and also Met-tRNAf bound to 40 S ribosomes in the presence of AUG codon but does not degrade Met-tRNAf in the ternary complex, Met-tRNAf.eIF-2.GTP. Purified Met-tRNAf deacylase does not inhibit protein synthesis in reticulocyte lysates at any concentration tested indicating that Met-tRNAf deacylase is not a protein synthesis inhibitor. Antibodies against Met-tRNAf deacylase have been prepared by immunizing a chicken with homogeneous preparation of Met-tRNAf deacylase. Addition of anti-Met-tRNAf deacylase does not have any effect on protein synthesis in reticulocyte lysates indicating that Met-tRNAf deacylase is not required for protein synthesis.
D000217:Acyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D019881:Aminoacyltransferases; D000818:Animals; D002645:Chickens / Q000276:immunology; D005033:Ethylmaleimide / Q000494:pharmacology; D007106:Immune Sera; D007118:Immunoassay; D007700:Kinetics; D008970:Molecular Weight; D009239:N-Formylmethionine / Q000302:isolation & purification / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000302:isolation & purification / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology*; D013379:Substrate Specificity
D007106:Immune Sera; D010448:Peptide Initiation Factors; D012346:RNA, Transfer, Amino Acyl; D009239:N-Formylmethionine; D000217:Acyltransferases; D019881:Aminoacyltransferases; C021560:methionyl-tRNA-Met-f deacylase; D005033:Ethylmaleimide