✦ LIBER ✦
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-ser/acetyl-thr) and homologies to similar mammalian isozymes
✍ Scribed by Jack R. Jabusch; Harold F. Deutsch
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 463 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.