Spinach carbonic anhydrase primary structure deduced from the sequence of a cDNA clone

T. W. Fawcett, J. A. Browse, M. Volokita, S. G. Bartlett

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Abstract

A cDNA clone 1,156 base pairs in length was selected by screening a λgt11 library with antibodies directed against spinach chloroplast carbonic anhydrase (carbonate dehydratase, EC 4.2.1.1). Sequence analysis revealed an open reading frame of 957 base pairs encoding a polypeptide containing 319 amino acids with a molecular weight of 34,569. This polypeptide is of sufficient size to represent the precursor of spinach chloroplast carbonic anhydrase. The polypeptide contains a sequence of 19 amino acids identical to the sequence of a cyanogen bromide fragment from spinach carbonic anhydrase. In addition, Escherichia coli was transformed with a plasmid that expresses spinach carbonic anhydrase. Lysates prepared from transformed E. coli contain acetazolamide-inhibitable carbonic anhydrase activity. The amino acid sequence of spinach carbonic anhydrase is distinct from those reported for the mammalian isozymes.

Original languageEnglish
Pages (from-to)5414-5417
Number of pages4
JournalJournal of Biological Chemistry
Volume265
Issue number10
StatePublished - 25 Apr 1990
Externally publishedYes

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