Skip to main content
. 2011 Dec;85(23):12721–12732. doi: 10.1128/JVI.00349-11

Table 2.

SEC analysis at different concentrations of NSP495-146 and ΔΝ94 purified under different conditionsa

Purification process Apparent molecular mass (no. of subunits)
SA11ΔΝ94 at concn (mg/ml) of:
ST3:NSP494-29 at concn (mg/ml) of:
10 5 20 10
Lysis in acidic pH 5.0 buffer (condition A) 60.25 (5.51) 47.86 (4.36) 34.9 (5.41) 27.21 (4.2)
Lysis in the absence of CaCl2 (condition B) 56.23 (5.14) 45.70 (4.08) 34.9 (5.41) 29.15 (4.5)
Lysis in the presence of CaCl2 (condition C) at concn (mM) of:
    0.1 57.54 (5.26) 50.12 (4.58) ND ND
    1.0 54.94 (5.02) 47.86 (4.38) ND ND
    10 57.54 (5.26) 48.97 (4.48) 33.69 (5.21) 27.86 (4.3)
Lysis and purification in the presence of 0.1 mM CaCl2 (condition D) 54.94 (5.02) 47.86 (4.38) 31.75 (4.95) 25.9 (4.0)
Lysis in the presence of 10 mM MgCl2 (condition E) 54.94 (5.02) 47.86 (4.36) ND ND
27.54 (2.52)
Lysis and purification in the presence of 0.1 mM MgCl2 (condition F) 60.2 (5.51) 47.89 (4.38) 32.69 (5.0) 25.9 (4.0)
a

Shown are the apparent molecular masses (numbers of subunits) corresponding to the major peaks of the SA11ΔN94 and ST3:NSP495-146 peptides purified under different conditions. Conditions A to F represent different conditions of purification. ND, not determined.