The Intrinsic Viscosity of Mixed Protein Systems, Including Studies of Plasma and Serum

Abstract

Experimental evidence is presented that the intrinsic viscosity of solutions of mixed proteins obeys the additive equation See PDF for Equation. The datum serves to characterize the system, and combined with other analytical techniques and fractionation procedures, enables one to analyze and characterize subfractions. The plasmas and sera of clinically "normal" individuals give intrinsic viscosity values agreeing with calculated values. The intrinsic viscosity values for pathological plasmas and sera in all cases are greater than normal and reflect the augmented levels of those proteins fibrinogen, α2-globulins, and γ-globulins occurring in the pathological state. The method is readily adaptable to routine clinical use and furnishes a measure of the departure from normal of protein levels in serum and plasma.

Mega macromolecules as single molecule lubricants for hard and soft surfaces

“…The intrinsic viscosity values of the mega HPGs are significantly lower than linear water-soluble polymers of similar molecular weight (e.g., PEO, hyaluronic acid, and dextran sulfate) 25,[32][33][34][35] , and this observation further confirms the compact nature of the mega HPGs. For example, the mega HPG-3 (9.3 MDa) possesses an intrinsic viscosity of 6.15 mL/g that is similar to most of the globular proteins in aqueous solutions [36][37][38] , whereas a linear PEG (M w 11 MDa) has a value of 2600 mL/g 28 . Thus, mega HPGs show a unique combination of ultra-high molecular weight, compact size, and very low intrinsic viscosity almost independent of molecular weight.…”

Factors Affecting the Viscosity in High Concentration Solutions of Different Monoclonal Antibodies

“…The viscosity coefficients describing the properties of a protein solution system are, therefore, a function of several variables. A few among these are: (i) the viscosity coefficient of the solvent, (ii) temperature of the solution, (iii) pH of the solution, (iv) ionic strength of the solution, (v) the velocity gradient under which viscosity coefficient was measured, (vi) concentration of the solute, (vii) electric charge on the molecule, (viii) physical interaction between macromolecules, (ix) the solvation of the molecule and (x) the shape of the macromolecule 40. The present study focuses on the effect of factors (v) to (x) on protein solution viscosity, while maintaining factors (i) to (iv), that is, the solvent, temperature, pH, and ionic strength constant.…”

Fluorescein-Conjugated Bovine Albumin

“…in a Svedberg oil turbine ultracentrifuge. Intrinsic viscosity determinations (7) (0.15 ~a NaC1, pH 5.2, 37.0 -4-0.05°C., Ostwald viscometer) were made on BAC preparations 5, 6, 7, 8. Within the limits of error of the method, the intrinsic viscosity (H) of BAC 6, 7, 8 was identical with that of bovine serum albumin (H = 0.042 dl./gm.).…”