F. Kerfourn et al., CHARACTERIZATION OF A MULTIMERIC POLYPEPTIDE COMPLEX ON THE SURFACE OF THYMUS-DERIVED CELLS IN THE MEXICAN AXOLOTL, Scandinavian journal of immunology, 38(4), 1993, pp. 381-387
We previously raised a rabbit antiserum (L12) against a 38 kD polypept
ide which is expressed on the surface of thymocytes and peripheral T c
ells of an Urodele Amphibian, the Mexican axolotl (Ambystoma mexicanum
). Here we show that L12 antibodies immunoprecipitate several labelled
molecules from surface iodinated axolotl spleen cells, including the
38 kD molecule, but also two polypeptides of 43 and 22 kD which are co
valently linked to other elements. Another rabbit antiserum (L10) was
raised against detergent-solubilized axolotl thymocyte membranes and s
hown to recognize the majority of thymocytes and about half of the spl
enocytes in immunofluorescence. In Western blotting, L10 antibodies re
cognized a limited number of surface polypeptides in thymocyte and spl
enocyte lysates, including 43, 38, and 22 kD elements. Immune complexe
s formed between L10 antibodies and solubilized splenocyte membranes w
ere used to immunize BALB/c mice intrasplenically in the aim of raisin
g MoAbs specific for axolotl T cells. Monoclonal antibody 87.16 was sh
own to stain in immunofluorescence 26.7% of thymocytes and 26.8% of sp
leen cells. This MoAb recognized a 43 kD polypeptide that can covalent
ly associate on the T-cell surface with several other molecules to for
m a multimeric complex.