Abstract
Lipopolysaccharide (LPS) was isolated from an acapsular strain of Erwinia amylovora . This “crude LPS” was divided into 2 fractions by elution from a Sepharose CL-6B column. These were designated the low molecular weight form (retained by the column) and the high molecular weight form (not retained by the column). When assayed by rocket electrophoresis, only the low molecular weight form served as a receptor for the apple agglutination factor (AF) and cross-reacted with antiserum prepared to E. amylovora . Mild acid hydrolysis of crude LPS gave a milky suspension that was divided into a pellet (Lipid A) and a supernate (O-side chain plus core) by centrifugation. The supernate, which contained all of the receptor for AF, was further divided into O-side chain and core by elution from a Bio-Gel P-30 column. Only those fractions which would be expected to contain core region of LPS interacted with AF in agarose gel to form precipitant peaks.
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