TABLE 1.
Protein | Theoretical mol wta (kDa) | Purityb (%) | Yieldc (mg/g) | Tm (°C) | HPLC-SEC |
||
---|---|---|---|---|---|---|---|
Peak retention time(s) (min) | Mol wt (kDa)d | Oligomeric state | |||||
CssA fusions | |||||||
dscACssA | 18.5 | 95 | 1.3 | 55 | 10.4 | 20.9 | Monomeric |
dscACssAA | 34.0 | 95 | 1.3 | 49.9, 75.3 | 9.3 | 34.2 | Monomeric |
dscBCssAB | 35.0 | 98 | 8.9 | 58.8, 74.5 | 7.5, 8.0, 9.2 | 45.7, 94.6 | Multimeric |
dscACssABA | 50.4 | 95 | 2.1 | 54.3, 75 | 8.5 | 59.2 | Monomeric |
dscBCssABB | 51.3 | 94 | 4.0 | 59.5, 74 | 7.2, 7.5, 8.5 | 67.4, 132 | Multimeric |
Refined CssAB fusions | |||||||
dscACssAB | 34.8 | 97 | 4.9 | 70 | 9.2 | 35.5 | Monomeric |
ntd_dscBCssAB | 33.3 | 99 | 3.8 | 59, 74.6 | 9.3 | 34.1 | Monomeric |
ntd_dscACssAB | 33.2 | 97 | 3.7 | 69.7, 76.1 | 9.4 | 33.9 | Monomeric |
CssB fusions | |||||||
dscBCssB | 19.4 | 91 | 3.1 | 60.1 | 10.4 | 22.5 | Monomeric |
dscBCssBB | 35.8 | 100 | 2.7 | 58, 92.6 | 8.1, 9.2 | 37.5, 94 | Multimeric |
dscACssBA | 34.8 | 91 | 4.3 | 69.2, 74.7 | 7.7, 8.2, 9.5 | 39.8, 93 | Multimeric |
dscACssBAA | 50.4 | 90 | 1.0 | 71.8, 77.6 | 7.1, 8.0 | 141 | Multimeric |
dscBCssBAB | 51.3 | 89 | 1.2 | 59.7, 75.5 | 7.6, 8.0, 8.6 | 63.1 | Multimeric |
dscACssBBA | 51.2 | 91 | 0.5 | 59, 71.4, 76 | 7.2, 7.9, 8.9 | 65.4, 122.7 | Multimeric |
Refined CssBA fusions | |||||||
dscBCssBA | 35.0 | 97 | 8.2 | 74.1 | 9.4 | 37.3 | Monomeric |
ntd_dscACssBA | 33.2 | 97 | 0.5 | 76.1 | 9.4 | 33.7 | Monomeric |
ntd_dscBCssBA | 33.3 | 98 | 3.0 | 74.7 | 9.3 | 33.9 | Monomeric |
The theoretical molecular weight of each protein was determined from the primary amino acid sequence.
Protein purity was determined by densitometric measurements of the protein separated on an SDS-PAGE gel.
Milligrams of protein obtained per gram of wet bacterial cell paste lysed.
The experimental molecular weight was determined using the refractive index of molecules eluting from the HPLC-SEC column.