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Amino Acid Sequence of Rabbit Carbonic Anhydrase II

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Specialties Biochemistry
Biophysics
Date 1978 Mar 28
PMID 416851
Citations 1
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Abstract

The amino acid sequence of the high activity form of erythrocyte carbonic anhydrase, carbonic anhydrase II, purified from rabbit erythrocytes has been determined. This sequence was determined primarily from the cyanogen bromide and tryptic peptides through use of automated Edman degradation procedures. The ordering of the peptides from rabbit carbonic anhydrase II was based on the high degree of homology between the rabbit enzyme and the homologous enzymes derived from sheep, bovine, and human erythrocytes. The function of certain residues is discussed in the context of these three known sequences and the previously reported three-dimensional structure of human carbonic anhydrase II. Possible microheterogeneity of rabbit carbonic anhydrase II is also discussed.

Citing Articles

Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.

Jabusch J, DEUTSCH H Biochem Genet. 1984; 22(3-4):357-67.

PMID: 6428393 DOI: 10.1007/BF00484234.