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Biomedical subjects

H Bleeg

Publications and source records attributed to H Bleeg.

5 recordsLinked to original sources
PubMed1990

Characterization of two types of human oral fibroblast with a potential application to cellular toxicity studies: tooth pulp fibroblasts and buccal mucosa fibroblasts.

Cultures of human oral buccal mucosa fibroblasts and human tooth pulp fibroblasts were established and grown under standard routine conditions. The biological characteristics of cell proliferation, growth pattern, cell morphology and enzyme release (lactate dehydrogenase and acid phosphatase) were studied. Under the same standard in vitro conditions the two cell types demonstrated different growth patterns and different levels of enzyme activity. It is suggested that differences in biological characteristics should be considered when selecting appropriate cells for toxicological studies of dental materials.

Acid Phosphatase↗
PubMed1983

Molecular biology of Haemophilus influenzae IgA1 proteases.

IgA1 proteases of two distinct specificities were demonstrated among 95 isolates of Haemophilus influenzae and nine isolates of H. aegyptius. The two enzymes cleaved two different peptide bonds in the hinge region of the alpha chain of IgA1: a prolyl-seryl bond located at position 231-232 (type A cleavage) and a prolyl-threonyl peptide bond between residues 235 and 236 (type B cleavage). Each strain of H. influenzae produced either one or both of these types of enzymes, whereas all H. aegyptius strains produced type A enzyme only. The application of enzyme-neutralizing antibodies to the study of IgA1 proteases produced by the 104 strains of H. influenzae and H. aegyptius revealed at least 15 different types of protease activities based on inhibition patterns in nine selected antibody preparations. The types of IgA1 proteases closely correlated with the serotype of encapsulated strains of H. influenzae. The study suggests that H. influenzae strains produce at least two serologically different IgA1 proteases with distinct or identical enzymatic activities.

Amino Acid Sequence↗