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Query: EC:6.1.1.12 (aspartyl-tRNA synthetase)
233 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The crystallizable cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae is a dimer made up of identical subunits (Mr 63 000). Its primary structure was established using peptide sequences from four different digests of the native and citraconylated enzyme with trypsin, cyanogen bromide and staphylococcal protease. The oligonucleotide sequence of the structural gene was used as a template for the final alignment of the various peptides in the correct order.
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PMID:The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. 390 99

Tryptic and cyanogen bromide peptides derived from yeast aspartyl-tRNA synthetase and from Escherichia coli ribosomal proteins were separated by reversed-phase liquid chromatography, employing volatile buffers of low ionic strength. The conditions used allow the performance of micro-sequencing without desalting or extensive lyophilization, and can therefore be applied to peptide mixtures containing hydrophobic fragments which tend to precipitate. To prevent losses of peptides, direct ultra-violet detection of the peptides was preferred, to detection by post-column derivatization with an additional stream splitting device. Preparative separations were performed with 5-10 nmol of peptide mixture; analytical runs were made with 5-10 micrograms of protein hydrolysate.
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PMID:Reversed-phase liquid chromatography of peptides for direct micro-sequencing. 634 6

The cristallizable aspartyl-tRNA synthetase from Baker's yeast is a dimer made up of identical subunits (Mr 60,000). We report here the results of tryptic digestion and cyanogen bromide cleavage which enabled us to align two lon stretches of sequence of 106 and 111 amino acids, respectively.
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PMID:Primary structure of aspartyl-tRNA synthetase from baker's yeast: tryptic and CNBr peptides. 641 27