Table 2.
Characteristics of proteins.
| Proteins a | Pi b | Charge c | ζ d, [mV] | MM e, [kDa] | Hydrophobicity f |
|---|---|---|---|---|---|
| BSA | 4.7 | −14 | −28 | 66 | 30 |
| Af2 | 5.3 | −16 | −28 | 37 | 33 |
| Ins | 5.4 | −4 | −9 | 5 | 39 |
| SWM | 7.6 | +2 | +5 | 17 | 37 |
| Lys | > 11 | +14 | +12 | 14 | 31 |
a Proteins used: BSA, bovine serum albumin; Af2, Asp f 2 from Aspergillus fumigatus; Ins, human insulin; SWM, sperm whale myoglobin; Lys, chicken lysozyme. b PI, isoelectric point is taken from the literature. c Charge is determined by calculating positive and negative amino acids. d Zeta potential was determined as described in Methods. e MM, molecular weight, kilodaltons. f Hydrophobicity is determined by calculation of percentage of hydrophobic acids using Vector NTI® Software (Life Technologies, Grand Island, NY, USA).