Alber, Birgit E.2014-03-142014-03-141995-06-09etd-06062008-171625http://hdl.handle.net/10919/38486Carbonic 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.xiii, 153 leavesBTDapplication/pdfenIn Copyrightcarbonic anhydraseCALD5655.V856 1995.A438Dissertationhttp://scholar.lib.vt.edu/theses/available/etd-06062008-171625/