The primary amino acid sequence of rabbit muscle enolase has been determined by standard spinning-cup sequencing techniques applied to peptides produced by chemical (cyanogen bromide and mild acid hydrolysis) and enzymatic fragmentation of the enzyme. The 433 amino acid sequence has been compared to other available enolase sequences from eukaryotic and prokaryotic sources, confirming a high degree of conserved sequence identity; the three mammalian muscle sequences (mouse and rat deduced from c-DNA sequences and rabbit) show 94% identity.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The primary amino acid sequence of rabbit muscle enolase has been determined by standard spinning-cup sequencing techniques applied to peptides produced by chemical (cyanogen bromide and mild acid hydrolysis) and enzymatic fragmentation of the enzyme. The 433 amino acid sequence has been compared to other available enolase sequences from eukaryotic and prokaryotic sources, confirming a high degree of conserved sequence identity; the three mammalian muscle sequences (mouse and rat deduced from c-DNA sequences and rabbit) show 94% identity.
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| skos:exactMatch | |
| uniprot:name |
J. Protein Chem.
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| uniprot:author |
Chin C.C.Q.
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| uniprot:date |
1990
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| uniprot:pages |
427-432
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| uniprot:title |
The primary structure of rabbit muscle enolase.
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| uniprot:volume |
9
|
| dc-term:identifier |
doi:10.1007/BF01024618
|