bromochloroacetic-acid and metaperiodate

bromochloroacetic-acid has been researched along with metaperiodate* in 2 studies

Other Studies

2 other study(ies) available for bromochloroacetic-acid and metaperiodate

Article	Year
The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct binding domains. FEMS microbiology letters, 1997, Aug-15, Volume: 153, Issue:2 In order to investigate the binding properties of the antigen I/IIf from Streptococcus mutans, we analyzed the binding activity of five I/IIf derivatives expressed by I/IIf gene derivatives obtained by insertion of a kanamycin resistance marker. ELISA-derived binding assays showed that the derivatives containing both the N-terminal alanine-rich domain (A-region) and an A-region distal domain extending to amino-acid 766 were the most effective in binding biotinylated (Biot-) human salivary components (SAC) and Biot-epithelial cell membrane components. Sodium metaperiodate treatment of SAC inhibited these interactions, suggesting a binding specificity of the A-region distal domain for carbohydrate residues. All the I/IIf derivatives were found to bind Biot-type I collagen, Biot-laminin, Biot-keratin, and Biot-fibronectin, the derivatives containing the A-region but lacking the A-region distal domain exhibiting the highest binding levels. Sodium metaperiodate treatment of laminin had no effect on its binding to the derivatives, suggesting that carbohydrate residues of the ligand were not involved. Topics: Antigens, Bacterial; Bacterial Adhesion; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carbohydrate Metabolism; Cell Membrane; Epithelial Cells; Epithelium; Escherichia coli; Extracellular Matrix Proteins; Humans; Keratins; Ligands; Membrane Glycoproteins; Periodic Acid; Protein Binding; Recombinant Proteins; Saliva; Streptococcus mutans	1997
Production of a human monoclonal antibody to normal basal and squamous cell carcinoma-associated antigen. Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 1993, Volume: 22, Issue:10 A human monoclonal antibody, BM2, was produced by a hybridoma line generated by fusion of lymph node cells from a patient with squamous cell carcinoma (SCC) of the tongue with human B-lymphoblastoid cell line HO-323. BM2, an IgM class antibody, was reactive with all of the SCC cell lines tested. Frozen sections of normal and malignant tumor specimens were investigated to examine the reactivity of BM2 towards them. All 35 oral SCC specimens reacted with BM2. Normal stratified squamous epithelium showed positive staining in basal cells, but no staining was seen in other layers of the stratified epithelium, simple epithelium, and tissues of nonepithelial origin. Ductal basal cells of normal salivary gland also showed positive staining. Western blotting and immunoprecipitation analysis revealed that BM2 recognized 52 kDa membrane-associated protein. BM2 may therefore be a useful tool for biological and clinical studies of SCC. Topics: Adenocarcinoma; Antibodies, Monoclonal; Antigens, Neoplasm; Carcinoma, Squamous Cell; Epithelial Cells; Epithelium; Fluorescent Antibody Technique; Formaldehyde; Humans; Hybridomas; Immunoglobulin Isotypes; Immunoglobulin M; Immunohistochemistry; Keratins; Membrane Proteins; Mitosis; Mouth Mucosa; Neuraminidase; Periodic Acid; Pronase; Submandibular Gland; Tumor Cells, Cultured	1993

Article

Year

The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct binding domains.

FEMS microbiology letters, 1997, Aug-15, Volume: 153, Issue:2

In order to investigate the binding properties of the antigen I/IIf from Streptococcus mutans, we analyzed the binding activity of five I/IIf derivatives expressed by I/IIf gene derivatives obtained by insertion of a kanamycin resistance marker. ELISA-derived binding assays showed that the derivatives containing both the N-terminal alanine-rich domain (A-region) and an A-region distal domain extending to amino-acid 766 were the most effective in binding biotinylated (Biot-) human salivary components (SAC) and Biot-epithelial cell membrane components. Sodium metaperiodate treatment of SAC inhibited these interactions, suggesting a binding specificity of the A-region distal domain for carbohydrate residues. All the I/IIf derivatives were found to bind Biot-type I collagen, Biot-laminin, Biot-keratin, and Biot-fibronectin, the derivatives containing the A-region but lacking the A-region distal domain exhibiting the highest binding levels. Sodium metaperiodate treatment of laminin had no effect on its binding to the derivatives, suggesting that carbohydrate residues of the ligand were not involved.

Topics: Antigens, Bacterial; Bacterial Adhesion; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carbohydrate Metabolism; Cell Membrane; Epithelial Cells; Epithelium; Escherichia coli; Extracellular Matrix Proteins; Humans; Keratins; Ligands; Membrane Glycoproteins; Periodic Acid; Protein Binding; Recombinant Proteins; Saliva; Streptococcus mutans

1997

Production of a human monoclonal antibody to normal basal and squamous cell carcinoma-associated antigen.

Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 1993, Volume: 22, Issue:10

A human monoclonal antibody, BM2, was produced by a hybridoma line generated by fusion of lymph node cells from a patient with squamous cell carcinoma (SCC) of the tongue with human B-lymphoblastoid cell line HO-323. BM2, an IgM class antibody, was reactive with all of the SCC cell lines tested. Frozen sections of normal and malignant tumor specimens were investigated to examine the reactivity of BM2 towards them. All 35 oral SCC specimens reacted with BM2. Normal stratified squamous epithelium showed positive staining in basal cells, but no staining was seen in other layers of the stratified epithelium, simple epithelium, and tissues of nonepithelial origin. Ductal basal cells of normal salivary gland also showed positive staining. Western blotting and immunoprecipitation analysis revealed that BM2 recognized 52 kDa membrane-associated protein. BM2 may therefore be a useful tool for biological and clinical studies of SCC.

Topics: Adenocarcinoma; Antibodies, Monoclonal; Antigens, Neoplasm; Carcinoma, Squamous Cell; Epithelial Cells; Epithelium; Fluorescent Antibody Technique; Formaldehyde; Humans; Hybridomas; Immunoglobulin Isotypes; Immunoglobulin M; Immunohistochemistry; Keratins; Membrane Proteins; Mitosis; Mouth Mucosa; Neuraminidase; Periodic Acid; Pronase; Submandibular Gland; Tumor Cells, Cultured

1993