ADSORPTION AND COVALENT IMMOBILIZATION OF HUMAN SERUM-ALBUMIN (HSA) AND GAMMA-GLOBULINS (GAMMA-G) ONTO POLY(STYRENE ACROLEIN) LATEXES WITH PYRENE, DANSYL, AND 2,4-DINITROPHENYL LABELS/

The poly(styrene/acrolein) latexes (P(SA)1 and P(SA)2), differing in p oly(acrolein) content, were synthesized by the emulsifier-less emulsio n-precipitation polymerization of styrene and acrolein. The fraction o f poly(acrolein) in the surface layer was 0.35 and 0.50, for the P(SA) 1 and P(SA)2 latex, respectively. Latexes were labelled with 2, 4-dini trophenylhydrazine (DNPH), dansylhdrazine (DAH), and 1-aminopyrene (AP Y). Surface concentration of labels Varied from 4.20.10(-7) mol m(-2) (for APY label on P(SA)1 latex) to 1.54.10(-6) mol m(-2) (for DNPH lab el on P(SA)2 latex) reflecting the fraction of polyacrolein in the sur face layer and bulkiness of the label. The differences between adsorpt ion and covalent immobilization of human serum albumin and gamma globu lins onto the P(SA)2 latex and onto its derivatives labelled with the 2,4-dinitrophenyl (DNP), dansyl (DA), and pyrene (PY) groups were smal l. The observation conforms to the hypothesis that polyacrolein forms domains on the surface of the P(SA) latexes and that after labelling s ome aldehyde groups are still available for the covalent immobilizatio n of proteins. Labelled and parent latexes were used in the model slid e and turbidimetric aggregation tests for the goat anti-HSA. The fluor escent latexes, labelled with APY and DAH, and latexes labelled and wi th DNPH were found to be suitable for the model tests, similarly as th e nonlabelled ones, however, some differences in the sensitivity, depe nding on the presence and the nature of labels, were noticed. The stan dard goat anti-HSA serum (Sigma) was detected at maximum dilution equa l to 2000 in the slide test, and in the dilution region from 1.8.10(3) to 4.7.10(6) times in the turbidimetric test.