A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions

Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

“…Moreover, the values of [η] obtained for some mammalian IgG immunoglobulins [12] lie within the range of [η] = (6-14)×10 −3 m 3 /kg reported in the literature [22]. The numerical values of [η] and k 1 for OSA are presented in Table III.…”

“…In the present paper, the discussion of the viscosity-temperature relationship of OSA solutions is limited only to the modified Arrhenius formula. It was quite recently successfully applied to several proteins [10][11][12][13][14], and has the form:…”

“…However, even for small concentrations the dependence of η sp /c versus concentration is not perfectly linear, so the linear extrapolation can give a serious error in [η] and k 1 [26]. The alternative method presented above was earlier successfully applied to several proteins [10][11][12][13][14]. It is worth noting that the numerical values of the intrinsic viscosity calculated from relation (10) at t = 25…”

“…Because the hydrodynamic interactions for different liquids and solutions are different, the numerical values of k 1 published in the literature [10][11][12][13][14]26] vary widely. As is seen in Table III, for OSA k 1 increases monotonically with increasing temperature.…”

Multi‐criteria manufacturability indices for ranking high‐concentration monoclonal antibody formulations

“…These can be attributed to the higher propensity of antibodies to form soluble aggregates and to be more viscous at high concentrations given the higher probability for protein‐protein interactions (Arakawa and Timasheff, 1985; Shire, 2009; Shire et al, 2004; Treuheit et al, 2002). For example, it has been reported that viscosity values above 10 cP were observed with mAbs at concentrations above 100–150 mg mL −1 (He et al, 2010a; Monkos and Turczynski, 1999; Patapoff and Esue, 2009). …”