Carbonic anhydrase is a ubiquitous zinc-metalloenzyme that catalyzes the interconversion of carbon dioxide and carbonate and has been found to play a wide range of roles in animals, plants and bacteria. Cotton genomic and cDNA libraries were screened for the plastidial isoform of carbonic anhydrase. The nucleotide sequences of two 1.2 Kb partial cDNA clones were determined. These clones exhibit high homology to carbonic anhydrases from other dicot plants and possess all the expected peptide motifs. For example, serine and threonine rich chloroplastic targeting peptide and conserved zinc binding residues are both present. These clones were utilized to isolate two carbonic anhydrase genes that were shown to encode different isoforms by PCR and RFLP analysis.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc279044 |
| Date | 12 1900 |
| Creators | Local, Andrea |
| Contributors | Benjamin, Robert C., Chapman, Kent Dean, O'Donovan, Gerard A. |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | ix, 109 leaves : ill., Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Local, Andrea |
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