Autor: |
Perryman MB, Kerner SA, Bohlmeyer TJ, Roberts R |
Jazyk: |
angličtina |
Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1986 Nov 14; Vol. 140 (3), pp. 981-9. |
DOI: |
10.1016/0006-291x(86)90732-1 |
Abstrakt: |
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: |
MEDLINE |
Externí odkaz: |
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