Skip to main content
. 2018 Jul 13;7:e37439. doi: 10.7554/eLife.37439

Figure 4. SDS-PAGE and Western blot of HdLbpA2.

Lanes 1, 2, 3 and 4 were loaded with 20 ng of pure recombinant HdLbpA2 stemming from pET- or pBBR1p264-based expression as indicated. Lanes 5 to 8 were loaded with extracts (15–20 μg protein) H. denitrificans wildtype grown on methylamine plus thiosulfate (MA + S2O32-), dimethylsulfide (DMS) and methylamine (MA). Lane 9 was loaded with extract (17.5 μg protein) of H. denitrificans expressing plasmid-encoded genes dsrEhdrC1B1AhyphdrC2B2hyplbpA from a constitutive promoter. Lanes 1 and 2 show silver stained gels. Western blots were developed with antiserum against HdLbpA2 or with anti-lipoic acid antibody as indicated.

Figure 4.

Figure 4—figure supplement 1. Purification of LbpA and LplA-like proteins and analysis of T. sibirica LbpA1 by gel permeation chromatography on Superdex 75.

Figure 4—figure supplement 1.

(A) Purification of LbpA and LplA-like proteins. Lane 1, LbpA1 from T. sibirica; lane 2, LbpA2 from H. denitrificans; lane 3, LplA from Thioalkalivibrio sp. K90mix; lane 4, LplA from H. denitrificans. (B) Analysis of T. sibirica LbpA1 by gel permeation chromatography on Superdex 75. Buffer: 20 mM sodium phosphate, pH 7.4 containing 150 mM NaCl. Protein elution peaked at 79 ml corresponding to a mass of 16–18 kDa. The protein thus behaved as a monomer.