1. A method is described for the simultaneous isolation of both Factor X and prothrombin from bovine plasma. The proteins are adsorbed on and eluted from barium sulphate and chromatographed on DEAE-Sephadex and are finally purified by rechromatography on DEAE-Sephadex. 2. The proteins can be purified in 48h from the collection of the blood and the method can be used to process large volumes of plasma. 3. The prothrombin has a molecular weight of 70300; the Factor X, on the other hand, is polydisperse, with most of the protein (86%) having a molecular weight of 56000.

Solutions of crystalline beta-lactamase I and beta-lactamase II, prepared by Kuwabara (1970), were examined in the ultracentrifuge and their sedimentation coefficients, diffusion coefficients, molecular weights and heterogeneity determined. Each sample was shown to consist of a major component comprising at least 97% of the material and a minor component of much higher molecular weight. The molecular weights of the major components were 27800 for beta-lactamase I and 35600 for beta-lactamase II. Emphasis is placed on a straightforward practical way of analysing the sedimentation-equilibrium results on mixtures of two macromolecular components rather than on a strict theoretical solution. Appendices describe the theory of systems at both chemical and sedimentation equilibrium and the procedure for calculating the combined distribution of two components.

Interaction between surfactants forms micelles that typically lead to a reduction of the irritation potential of the mixture. The objective of this study is to illustrate that such antagonism between surfactants is applicable to actual cases of consumer products e.g. laundry detergent products. The Zein test is an in vitro assay measuring corn protein denaturation by solutions of surfactant(s) and often used to predict their acute irritation potential. The Zein test data for the surfactant mixtures from nine representative laundry detergents demonstrate that the protein denaturation by the mixtures is, in all cases, lower than the cumulative score of protein denaturation by the different surfactants tested separately. The data clearly indicate that antagonism occurs between the actual surfactants present in their exact proportions as found in the consumer laundry detergent products. These data support the view that the hazard classification of detergent products as (irritant) by the dangerous preparation directive should not be based on a simple cumulative score of the irritation properties of the individual components of the products.

A method is described of using photography to measure the concentrations of a small ligand (proflavine) above and below the boundary of a macromolecule (DNA, both native and denatured) sedimenting in the ultracentrifuge. The measurements are used to determine the extent of the binding of proflavine to DNA, and the results compared with those obtained by a spectrophotometric method. The results obtained by the two methods agree within 10%, thus validating the spectrophotometric technique under these conditions. The variation of the sedimentation coefficient with the extent of binding of proflavine was also studied. The results are discussed in relation to previously observed changes in the viscosity of the solutions.