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Identification of in vivo Pellicle Constituents by Analysis of Serum Immune Responses

¹ Department of Periodontology and Oral Biology, Boston University Goldman School of Dental Medicine, 700 Albany Street, Boston, MA 02118, USA; and
² Department of Biochemistry, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA;

View larger version (32K): [in a new window]   Figure 1. Reactivities of mouse anti-pellicle antiserum against purified protein standards in ELISA. Pre- and post-immune sera were collected from 2 mice before the first injection with pellicle and ten days after the 4th boost with pellicle proteins, respectively. Microtiter plates were coated with pellicle proteins (10 µg/mL) or a series of purified protein standards (2 µg/mL) and subsequently incubated with 1:1000 diluted pre-immune serum (white bars) or 1:1000 diluted post-immune serum (black bars). Each bar represents the mean value ± SD of one experiment performed in triplicate. Panel A, mouse #1; Panel B, mouse #2.

View larger version (37K): [in a new window]   Figure 2. Immunoblotting of human pellicle, purified lysozyme, lactoferrin, carbonic anhydrase II, and PRP1 with specific antisera. Purified proteins (0.25 µg) or pellicle (40 µg) was subjected to Tris-tricine (Panels A-C) or Ornstein-Davis (Panel D) PAGE and blotted onto PVDF membranes. Panel A, blot was probed with 1:100 diluted anti-lysozyme anti-serum. Panel B, blot was probed with 1:250 diluted anti-lactoferrin anti-serum. Panel C, blots were probed with 1:1000 diluted anti-carbonic anhydrase II anti-serum. Panel D, blot was probed with 1:2000 diluted anti-PRP1 anti-serum. Upper arrow, large PRPs (PRP1, 2 and PIFs); lower arrow, small PRPs (PRP3, 4 and PIFf).