Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acyl-tRNA Synthetases* / metabolism
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Aspartate-tRNA Ligase* / metabolism
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Cyanogen Bromide
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Cytoplasm / enzymology
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Endopeptidases / metabolism
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Metalloendopeptidases*
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Peptide Fragments / metabolism
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Saccharomyces cerevisiae / enzymology*
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Trypsin / metabolism
Substances
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Peptide Fragments
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Endopeptidases
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Trypsin
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Metalloendopeptidases
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auR protein, Staphylococcus aureus
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Amino Acyl-tRNA Synthetases
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Aspartate-tRNA Ligase
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Cyanogen Bromide