Literature DB >> 416851

Amino acid sequence of rabbit carbonic anhydrase II.

R E Ferrell, S K Stroup, R J Tanis, R E Tashian.   

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.

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Year:  1978        PMID: 416851     DOI: 10.1016/0005-2795(78)90541-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

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

Authors:  J R Jabusch; H F Deutsch
Journal:  Biochem Genet       Date:  1984-04       Impact factor: 1.890

  1 in total

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