Detection of binding of denatured salivary alpha-amylase to Streptococcus sanguis.
Native alpha-amylase, either solubilized, or immobilized and tested with an overlay immunotechnique, was bound in a species-specific manner to Streptococcus mitis and to one of the Streptococcus gordonii strains. However, only insignificant amounts of alpha-amylase were bound to Streptococcus sanguis and all other strains tested. When alpha-amylase was denatured before immobilization, Streptococcus sanguis bound strongly to the protein while binding of other strains was insignificant.
Bergmann
J E
JE
Dept. of Conservative and Preventive Dentistry, University of Hamburg, Dental School, Germany.
Gülzow
H J
HJ
D001422:Bacterial Adhesion / Q000502:physiology*; D001665:Binding Sites; D006801:Humans; D011485:Protein Binding; D011489:Protein Denaturation; D012463:Saliva / Q000201:enzymology; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D013298:Streptococcus sanguis / Q000378:metabolism*; D000516:alpha-Amylases / Q000378:metabolism*
D012471:Salivary Proteins and Peptides; D000516:alpha-Amylases