Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified> 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from <i>Synechococcus</i> sp. strain PCC7942. / Ph. D.
| Identifer | oai:union.ndltd.org:VTETD/oai:vtechworks.lib.vt.edu:10919/38486 |
| Date | 06 June 2008 |
| Creators | Alber, Birgit E. |
| Contributors | Biochemistry and Anaerobic Microbiology, Ferry, James G., Dean, Dennis R., Johnson, John L., Gregory, Eugene M., Niehaus, Walter G. Jr. |
| Publisher | Virginia Tech |
| Source Sets | Virginia Tech Theses and Dissertation |
| Language | English |
| Detected Language | English |
| Type | Dissertation, Text |
| Format | xiii, 153 leaves, BTD, application/pdf, application/pdf |
| Rights | In Copyright, http://rightsstatements.org/vocab/InC/1.0/ |
| Relation | OCLC# 34489092, LD5655.V856_1995.A438.pdf |
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