TY - CHAP
T1 - Biochemical analysis of an MHC-linked hematopoietic cell surface antigen, Qa-2
AU - Soloski, M. J.
AU - Vitetta, E. S.
AU - Flaherty, L.
AU - Uhr, J. W.
PY - 1981
Y1 - 1981
N2 - The region of the murine 17th chromosome telomeric to H-2D encodes a group of serologically defined cell surface antigens termed Qa-1-5. These antigens are of interest because their expression is restricted to hematopoietic cells. In addition, the molecular weight and subunit structure (ie, association with β-2 microglobulin) of Qa-2 molecules are similar to H-2 and TL antigens. In the present studies, we have prepared isotopically labeled Qa-2 and H-2 molecules from mitogen-stimulated C57BL/6 spleen cells. Comparative peptide mapping of tryptic peptides from Qa-2 and H-2 molecules (K(b), D(b)K(k), D(d)) reveal that Qa-2 has a unique primary structure. However, considerable homology is indicated since 30-40% of the Qa-2 peptides cochromatograph with peptides derived from H-2K(b), H-2D(b), H-2K(k), and H-2D(d). Studies by other investigators have demonstrated that similar levels of structural homology are observed when H-2K, H-2D, and H-2L tryptic peptides are analyzed. We conclude from these studies that the Qa-2 alloantigen is structurally related to a class of cell surface molecules (ie, H-2) that play critical roles in immune recognition processes. These data further suggest that the genes encoding Qa-2 and H-2 molecules have arisen from a common primordial gene.
AB - The region of the murine 17th chromosome telomeric to H-2D encodes a group of serologically defined cell surface antigens termed Qa-1-5. These antigens are of interest because their expression is restricted to hematopoietic cells. In addition, the molecular weight and subunit structure (ie, association with β-2 microglobulin) of Qa-2 molecules are similar to H-2 and TL antigens. In the present studies, we have prepared isotopically labeled Qa-2 and H-2 molecules from mitogen-stimulated C57BL/6 spleen cells. Comparative peptide mapping of tryptic peptides from Qa-2 and H-2 molecules (K(b), D(b)K(k), D(d)) reveal that Qa-2 has a unique primary structure. However, considerable homology is indicated since 30-40% of the Qa-2 peptides cochromatograph with peptides derived from H-2K(b), H-2D(b), H-2K(k), and H-2D(d). Studies by other investigators have demonstrated that similar levels of structural homology are observed when H-2K, H-2D, and H-2L tryptic peptides are analyzed. We conclude from these studies that the Qa-2 alloantigen is structurally related to a class of cell surface molecules (ie, H-2) that play critical roles in immune recognition processes. These data further suggest that the genes encoding Qa-2 and H-2 molecules have arisen from a common primordial gene.
UR - http://www.scopus.com/inward/record.url?scp=0019776188&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019776188&partnerID=8YFLogxK
M3 - Chapter
C2 - 7299842
AN - SCOPUS:0019776188
VL - 16
SP - 167
EP - 177
BT - Journal of Supramolecular and Cellular Biochemistry
ER -