The interaction of a protein from the coelomic fluid of earthworms with staphylococcal protein A.
A Staphylococcal protein A (SpA)-binding protein was isolated from coelomic fluids of the annelids, Lumbricus terrestris (LT) and Eisenia foetida (EF), by affinity chromatography on SpA-Sepharose. Analyses by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) under reducing and nonreducing conditions showed that SpA-binding activity is associated with a single chain protein, with a mol wt of 62 kD. The carbohydrate moiety of this protein consists of 21.4 g/100 g of O-linked and N-linked oligosaccharides. The amino acid composition of SpA-binding protein did not show structural homology with that of human IgG1 heavy chain (Daw), which also binds SpA.
Rejnek
J
J
Department of Immunology, Czechoslovak Academy of Science, Prague.
Tucková
L
L
Zikán
J
J
Tomana
M
M
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001147:Arsanilic Acid / Q000276:immunology; D001826:Body Fluids / Q000378:metabolism; D002241:Carbohydrates / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D009835:Oligochaeta / Q000378:metabolism*; D012709:Serum Albumin / Q000276:immunology; D013205:Staphylococcal Protein A / Q000378:metabolism*
D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D012709:Serum Albumin; D013205:Staphylococcal Protein A; D001147:Arsanilic Acid