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Amino acid sequence of human erythrocyte carbonic anhydrase B

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
48
Issue
3
Identifiers
DOI: 10.1016/0006-291x(72)90400-7
Disciplines
  • Biology

Abstract

Abstract The amino acid sequence of human carbonic anhydrase B, the major form of the enzyme in human red cells, has been investigated using a strategy based upon restriction of tryptic hydrolysis to arginyl peptide bonds by reversible blocking of lysine side chains by amidination. A proposal is made for the complete sequence of the protein which consists of 260 amino acid residues in a single polypeptide chain devoid of disulfide bridges. From X-ray diffraction studies on a homologous form of the enzyme three histidine residues in the central portion of the polypeptide chain have been suggested as ligands to the zinc ion in the active site. The results obtained here provide support for this suggestion, at least for two of these ligands.

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