Interaction of alpha-agglutinin with Saccharomyces cerevisiae a cells.

Abstract:

:Binding of Saccharomyces cerevisiae alpha-agglutinin to target a cells was assayed by agglutination inhibition and 125I-alpha-agglutinin binding. The assays showed characteristics of equilibrium binding, namely saturability, competability, and the establishment of a kinetic endpoint in the presence of free alpha-agglutinin and free receptor. The binding was heterogeneous, displaying strong binding (10(9) liters/mol) and a weaker interaction. There were about 2 X 10(4) strong binding sites per a cell. Denaturing gels displayed identical labeled species binding to the a cells in the weak and strong interactions. Furthermore, weakly bound material could subsequently bind tightly to fresh a cells, implying that the same species of alpha-agglutinin was bound in the two states.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Lipke PN,Terrance K,Wu YS

doi

10.1128/jb.169.2.483-488.1987

subject

Has Abstract

pub_date

1987-02-01 00:00:00

pages

483-8

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

169

pub_type

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