[Peripheral T and B lymphocytes in patients with occupational medicamentosa-like dermatitis due to trichloroethylene].

Objective: To investigate the changes in liver function and peripheral regulatory lymphocytes before and after treatment in patients with occupational medicamentosa-like dermatitis due to trichloroethylene (OMDT) . Methods: In December 2019, 16 patients with OMDT (8 patients with erythema multiforme and 8 with erythema multiforme major) who were admitted from February 2017 to February 2019 were enrolled as subjects. Liver function parameters and percentages of peripheral regulatory lymphocytes were measured before and after treatment, and the changes in liver function and peripheral regulatory T and B lymphocytes and their correlation were analyzed. Results: Before treatment, compared with the healthy control group, the experimental group had significantly higher levels of alanine aminotransferase (ALT) , aspartate aminotransferase (AST) , total bilirubin (TBIL) , direct bilirubin (DBIL) and gamma-glutamyl transpeptidase (GGT) and significantly lower levels of total protein (TP) , albumin (ALB) and cholinesterase (CHE) (P<0.05) . Compared with the healthy control group, the experimental group had significantly lower percentages of lymphocytes, CD4(+) T cells, CD4(+)CD25(+) Tregs, CD19(+)CD24(+)CD27(+) Bregs and CD4(+)/CD8(+) ratio, as well as a significantly higher percentage of CD8(+) T cells (P<0.05) . Before treatment, the levels of ALT, AST, GGT and DBIL were negatively correlated with the percentages of CD4(+)CD25(+) Tregs, CD19(+)CD24(+)CD27(+) Bregs, CD4(+) T cells and CD4(+)/CD8(+) ratio (r=-0.386 to -0.809, P<0.05) and was positively correlated with the percentage of CD8(+) T cells (except DBIL) (r=0.503-0.568, P<0.05) . The levels of TP and ALB were positively correlated with the percentages of CD4(+)CD25(+) Tregs, CD19(+)CD24(+)CD27(+)Bregs and CD4(+) T cells (r= 0.351-0.784, P<0.05) , ALB was negatively correlated with the percentage of CD8(+) T cells (r=-0.315, P<0.05) . CHE was positively correlated with the percentages of CD4(+)CD25(+) Tregs, CD19(+)CD24(+)CD27(+)Bregs and CD4(+)/CD8(+) ratio (r=0.390-0.527, P<0.05) . Conclusion: Immune dysfunction is observed in patients with OMDT, which may be caused by the imbalance of regulatory lymphocytes. And liver injury may be associated with the increase of CD8(+) T cells and the reductions of percentages of CD4(+) T cells, CD4(+)CD25(+) Tregs, CD19(+)CD24(+)CD27(+)Bregs and CD4(+)/CD8(+) ratio.

Agar-based magnetic affinity support for protein adsorption.

Magnetic colloidal particles were prepared by a coprecipitation method. The particles were composed of nanometer-sized superparamagnetic Fe(3)O(4) particles stabilized by lauric acid. Then, magnetic agar gel beads were produced by a water-in-oil emulsification method using a mixture of agar solution and the magnetic colloidal particles as the aqueous phase. A reactive triazine dye, Cibacron blue 3GA (CB), was coupled to the gel to prepare an agar-based magnetic affinity support (MAS) for protein adsorption. The support showed good magnetic responsiveness in a magnetic field. Bovine serum albumin (BSA) was used as a model protein to test adsorption equilibrium and kinetic behavior of the MAS. The adsorption equilibrium of BSA to the MAS was described by the Langmuir-type isotherm. Adsorption capacity of the MAS for BSA was up to 25 mg/mL at a CB coupling density of 1.6 micromol/mL. The effect of ionic strength on BSA adsorption was complex, exhibiting a maximum capacity at an ionic strength of 0.06 mol/L. The adsorption of BSA to the MAS was also influenced by pH. Uptake rate of BSA to the MAS was analyzed using a pore diffusion model. The pore diffusion coefficient was estimated to be 1.75 x 10(-11) m(2)/s. Finally, recycled use of the MAS demonstrated the stability of the MAS in protein adsorption and magnetic responsiveness.

A novel magnetic affinity support for protein adsorption and purification.

A novel magnetic support was prepared by an oxidization-precipitation method with poly(vinyl alcohol) (PVA) as the entrapment material. Transmission electron microscopy indicated that the magnetic particles had a core-shell structure, containing many nanometer-sized magnetic cores stabilized by the cross-linked PVA. The particles showed a high magnetic responsiveness in magnetic field, and no aggregation of the particles was observed after the particles had been treated in the magnetic field. These facts indicated that the particles were superparamagnetic. Cibacron blue 3GA (CB) was coupled to the particles to prepare a magnetic affinity support (MAS) for protein adsorption. Lysozyme was used as a model protein to test the adsorption properties of the MAS. The adsorption equilibrium of lysozyme to the MAS was described by the Langmuir-type isotherm. The capacity for lysozyme adsorption was more than 70 mg/g MAS (wet weight) at a relatively low CB coupling density (3-5 micromol/g). In addition, 1.0 M NaCl solution could be used to dissociate the adsorbed lysozyme. Finally, the MAS was recycled for the purification of alcohol dehydrogenase (ADH) from clarified yeast homogenates. Under proper conditions, the magnetic separation yielded over 5-fold purification of the enzyme with 60% recovery of the enzyme activity.