Evidence that a glycolipid tail anchors antigen 117 to the plasma membrane of Dictyostelium discoideum cells
- St. Louis Univ. School of Medicine, MO (USA)
The authors describe the biochemical features of the putative cell cohesion molecule antigen 117, indicating that it is anchored to the plasma membrane by a glycolipid tail. Antigen 117 can be radiolabeled with ({sup 3}H)myristate, ({sup 3}H)palmitate, and ({sup 14}C)ethanolamine. The fatty acid label is removed by periodate oxidation and nitrous acid deamination, indicating that the fatty acid is attached to the protein by a structure containing carbohydrate and an unsubstituted glucosamine. As cells develop aggregation competence, the antigen is released from the cell surface in a soluble form that can still be radiolabeled with ({sup 14}C)ethanolamine but not with ({sup 3}H)myristate of ({sup 3}H)-palmitate. The molecular weight of the released antigen is similar to that found in the plasma membrane, but it preferentially partitions in Triton X-114 as a hydrophilic, as opposed to a hydrophobic, protein. Plasma membranes contain the enzyme activity responsible for the release of the antigen in a soluble form.
- OSTI ID:
- 5642058
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 85:15; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ANTIGENS
MOLECULAR WEIGHT
CELL MEMBRANES
CROSS-LINKING
LIPOPOLYSACCHARIDES
AMINES
CARBON 14 COMPOUNDS
GLUCOPROTEINS
GLUCOSAMINE
HEXADECANOIC ACID
TRITIUM COMPOUNDS
CARBOHYDRATES
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CHEMICAL REACTIONS
GLYCOPROTEINS
HEXOSAMINES
HEXOSES
HYDROGEN COMPOUNDS
LABELLED COMPOUNDS
LIPIDS
MEMBRANES
MONOCARBOXYLIC ACIDS
MONOSACCHARIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
POLYMERIZATION
POLYSACCHARIDES
PROTEINS
SACCHARIDES
550201* - Biochemistry- Tracer Techniques