Fig. 2
From: Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans
Purification of wt and truncated CaNce103p variants and detection of the oligomeric state of Δ29_CaNce103p. (a) 12% SDS-PAGE analysis of CaNce103p, ∆29_CaNce103p, ∆48_CaNce103p and ∆61_CaNce103p (b) Elution profile (A280) of Δ29_CaNce103p on a Superdex 200 Increase 10/300 GL. A 100 μl aliquot of a 1.0 mg/ml solution of Δ29_CaNce103p was injected. The column was equilibrated and run as described in the Methods section. Molecular weights of monomeric, dimeric and tetrameric forms were estimated by comparison with protein standards (Sigma Aldrich). The upper scale indicates elution volumes for Mw standards from left to right: blue dextran (2000 kDa), alcohol dehydrogenase (ADH, 141 kDa), bovine serum albumin (BSA, 66 kDa), α-carbonic anhydrase from bovine erythrocytes (CA, 29 kDa) and cytochrome C (CytC 12.4 kDa). Arrows with calculated molecular weights indicate elution volumes for Δ29_CaNce103p monomers, dimers and tetramers