Characterization of the alpha-amylase receptor of Streptococcus gordonii NCTC 7868.

Abstract:

:The purpose of the work described here was to investigate the mechanisms involved in the binding of salivary alpha-amylase to Streptococcus gordonii NCTC 7868 (Challis). Of six types of alpha-amylase studied, only mammalian forms of the enzyme were found to bind to S. gordonii cells. Salivary alpha-amylase binding was inhibited by treatment of cells with trypsin and pronase, but not with pepsin or sodium periodate. Presence of starch, dextrin, or maltoheptaose partially inhibited binding of the enzyme to S. gordonii. Both mutanolysin extracts of cells and culture supernatants contained alpha-amylase-binding activity, which was partially purified by Sepharose CL-6B and DEAE-ion-exchange chromatography. Western blotting detected four putative receptor bands--65 kDa, 15 kDa, 12.5 kDa, and one with a very high molecular weight; the lower-molecular-weight components may be products of proteolytic degradation of the high-molecular-weight material, but their true relationship has yet to be determined. Pre-treatment of salivary alpha-amylase with these putative receptors partially inhibited subsequent binding of the enzyme to S. gordonii cells. When bound to cells, only 19% of the salivary alpha-amylase activity was detectable, suggesting that alpha-amylase binds to the receptor at or near the active site of the enzyme.

journal_name

J Dent Res

authors

Douglas CW

doi

10.1177/00220345900690110701

subject

Has Abstract

pub_date

1990-11-01 00:00:00

pages

1746-52

issue

11

eissn

0022-0345

issn

1544-0591

journal_volume

69

pub_type

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