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KMID : 0364219890320040412
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Korean Journal of Zoology
1989 Volume.32 No. 4 p.412 ~ p.419
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Production of Monoclonal Antibody Against the Plasmalemma of Amoeba and its Application in Determining the Role of Membrane Components
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Ahn Tae-In
Choi Ji-Young
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Abstract
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Monoclonal antibodies (MAbs) reacting with the plasmalemma of Amoeba proteus were produced. Specificity of the 3 MAbs was determined by transfer blotting of the SDS polvacryfamide gel. AMS antibody reacted with the mucopolysaccharide bands of the spacer gel, 220 KD and 50 KD proteins of the resolving gel. The maior glycoprotein bands (175 KD, 165 KD) and 50 KD protein of the plasmalemma were recognized by AUG antibody. A third, AMP antibody reacted with the 50 KD protein only. In immunofluorescence microscopy of the enzyme treated cells, the antigens of these MAbs were sensitive to proteases, but not sensitive to neuraminidase. In the assay of cell to substratum attachment after binding with the antibody, AMG and AMP antibodies exerted no effect, but AMS hindered the attachment and cell spreading. Thus the effective components of the plasmalemma in cell to substratum attachment appear to be the mucopolysaccharides and 220 KD protein. The membranes of latex particle infested phagosomes did not show any distinction from the plasmalemma in fluorescence microscopy. Phagosome membranes of amoebae appear to be derived from the plasma membrane without selection in terms of the antigen composition.
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KEYWORD
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Monoclonal antibody , Attachment , Plasma membrane , Amoeba proteus
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