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.
Dept. of Conservative and Preventive Dentistry, University of Hamburg, Dental School, Germany.
J E
JE
Bergmann
H J
HJ
Gülzow
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