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Biomedical subjects

L Ostberg

Publications and source records attributed to L Ostberg.

46 records · Page 3Linked to original sources
PubMed1975

Evolutionary relationship between immunoglobulins and transplantation antigens.

The major human and murine histocompatibility antigens are tetrameric molecules with an apparent molecular weight of about 130,000. They are composed of two types of polypeptide chains. The two light chains, previously identified as beta2-microglobulins, are bound to the two heavy, alloantigenic HL-A or H-2 polypeptide chains by noncovalent interactions only. The heavy chains are held together by disulfide bridge(s) located in the part of the molecule that is attached to the cell membrane. By limited proteolysis of the histocompatibility antigens evidence was obtained suggesting that the heavy chain may consist of three compact domains connected by more extended stretches of polypeptide chain. Each domain appeared to contain a single disulfide bride encompassing about 60 to 70 amino-acid residues. Staphylococcus aureus protein A is known to bind exclusively to the Fe region of immunoglobulin G. It was, however, observed that protein A interacts in a similar way with the H-2 antigen heavy chain. This observation, together withthe homology of the primary structure of beta2-microglobulin to immunoglobulin G, the tetrameric structure of the alloantigens, the ogranizations of the heavy polypeptide chain into compact domains, and the presence of a single, immunoglobulin-like disulfide loop in each domain, establishes a close similarity in structure between histocompatibility antigens and immunoglobulins. The similarity in structural features suggests a common evolutionary origin of the two types of molecules.

Animals↗
PubMedDate not supplied

Nucleotide sequence of chimpanzee Fc and hinge regions.

The nucleotide sequence of the Fc and hinge regions of a chimpanzee monoclonal antibody has been determined. Most of the sequence is similar to the human IgG1 sequence. However, the chimpanzee hinge regions differs from the human hinge region in six of 48 nucleotides, which leads to three amino acid substitutions. Two of the amino acid changes are not conservative and may lead to differences in flexibility of the hinge. The chimp hinge sequence seems to be a combination of the human IgG1 hinge and the hinge sequence of a human IgG pseudogene. The implications of this difference for the evolution of human IgG subgroup is discussed. Despite differences in the hinge regions, the chimpanzee monoclonal antibody differs from the most closely related human IgG1 allotype only slightly more than the two most distantly related human allotypes differ from each other.

Amino Acid Sequence↗