The effects of strapped spectacles on the fit factors of three manufactured brands of full facepiece negative pressure respirators.

A study was conducted to determine the effects of strapped spectacles on the fit factors obtained during quantitative fit testing on three different brands of full facepiece negative pressure respirators. The three brands of respirators were evaluated with and without strapped spectacles worn by the test subjects. A total of 180 quantitative fit testing trials were conducted on ten male test subjects. For each test subject, three quantitative fit testing trials were performed with each brand of respirator with and without the spectacles. The average of the fit testing trials for each subject with each respirator was used for statistical analysis. The results demonstrated that the fit factor values were significantly lower during use of the spectacles (p < 0.05). The estimated percentage of test subjects who failed the American National Standards Institute pass/fail criteria for quantitative fit testing (1000) increased by 15-36% when spectacles were worn.

Solid-phase assay for determination of binding parameters of ligand-protein complexes with high dissociation rates.

The binding parameters, the affinity constant (Ka) and binding capacity (Q), of a protein possessing ligand-protein complexes with a high dissociation rate (Sex Steroid Binding protein from Bufo arenarum) were determined using a solid-phase method. The technique is based upon the adsorption of the steroid-protein complex to DEAE-cellulose. This method was compared with a nonequilibrium method (charcoal adsorption of free ligand), and the latter resulted in underestimation of both binding parameters, Ka and Q. The solid-phase method reported here is appropriate to determine the binding parameters of proteins with high dissociation rates because the results are independent of the complex half-time. The method also possesses advantages compared to other equilibrium assays such as dialysis or steady-state electrophoresis. With minor modifications, it may be useful to characterize different proteins, particularly those possessing ligand-protein complexes with very high dissociation rates.