Isolation and sequence analysis of a full-length cDNA for human M creatine kinase
| Autor: | Teresa J. Bohlmeyer, Robert Roberts, Sandra A. Kerner, M. Benjamin Perryman |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Untranslated region
Sequence analysis Biophysics Creatine Biochemistry chemistry.chemical_compound Species Specificity Sequence Homology Nucleic Acid Complementary DNA Animals Humans Coding region Amino Acid Sequence Creatine Kinase Molecular Biology Peptide sequence Sequence (medicine) Base Sequence biology DNA Cell Biology Molecular biology chemistry Genetic Code Protein Biosynthesis biology.protein Creatine kinase |
| Zdroj: | Biochemical and Biophysical Research Communications. 140:981-989 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(86)90732-1 |
| Popis: | A full length cDNA for human M creatine kinase has been isolated and sequenced. The cDNA contains 77 bp of 5' untranslated, 338 bp of 3' untranslated sequence and the entire coding region (1146 bp) for human M creatine kinase. The M creatine kinases from different species share considerable sequence homology within the coding region (77-91%) and in amino acid sequence (82-97%). Little or no sequence homology is observed in the 3' untranslated sequence of the mammalian M creatine kinases, although canine and human creatine kinase share overall 80% sequence homology in 5' untranslated sequence. A unique 8 bp sequence was identified in the 5' untranslated regions of mammalian M creatine kinase but is not present in B creatine kinase cDNA. The degree of sequence conservation observed implies an evolutionary constraint on M creatine kinase structure beyond that which would be expected for the maintenance of enzymatic function. |
| Databáze: | OpenAIRE |
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