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Biomedical subjects

M Potter

Publications and source records attributed to M Potter.

At least 343 records · Page 19Linked to original sources
PubMed1970

Immunoglobulin structure: amino terminal sequences of kappa chains from genetically similar mice (BALB/c).

The amino terminal portion of 20 kappa chains from the highly inbred BALB/c mouse has been examined on an automatic protein sequencer. These proteins can be divided into at least nine groups (subgroups) based on sequence patterns which are so distinct that each subgroup is probably encoded by at least one germ-line gene. The subgroups of mouse kappa chains are generally quite different from those of human kappa chains.

Amino Acid Sequence↗
PubMed1970

Common individual antigenic determinants in five of eight BALB-c IgA myeloma proteins that bind phosphoryl choline.

Eight IgA myeloma proteins derived from independently induced plasma-cytomas in genetically similar inbred BALB/c mice are functionally related by their binding of phosphoryl choline-containing antigens (Pneumococcus C polysaccharide or Lactobacillus antigen). Each protein resembles a single species of immunoglobulin in antibody. The proteins are characterized by highly sensitive myeloma-specific antisera prepared by immunizing mice of other inbred strains with the BALB/c myeloma proteins. Individual or myeloma-specific determinants located on Fab fragments were found on three of the proteins that were unique for that protein and did not react with any other IgA protein among over 70 tested. Remarkably, five of the proteins shared two common myeloma-specific determinants which were specific for this group of five proteins. These results suggest that the five functionally and genetically related proteins sharing the same myeloma-specific determinants might also be structurally similar.

Animals↗
PubMed1969

Crossing over between genes in the immunoglobulin heavy chain linkage group of the mouse.

Immunoglobulin heavy chain genes were found in wild mice (Mus musculus) that could best be explained as recombinants of immunoglobulin genotypes. In wild mice from Kitty Hawk, N. C., two new heavy chain linkage groups, G(3,5,7,8)H(9,11)F(f)A(-) and G(3,5,8)H(9,11)F(f)A(-), were found, each of which genetically controls both the 3 and 5 distinct immunoglobulin determinants. In inbred strains the 3 and 5 determinants are found independently. The new heavy chain allotype G(3,5,7,8)H(9,11)F(f)A(-) probably arose from a homologous (intragenic) cross-over between G(3,8)H(9,11)F(f)A(-) and G(5,7,8)H(9,11)F(f)A(14) heavy chain linkage groups. It was suggested that genes controlling G(3,8)G(5,7,8), G(3,5,8), and G(3,5,7,8) are alleles. Another homozygous wild mouse (Kyushu, Japan) showed a new heavy chain allotype, (2)G(1,6,7,8)H(9,16)F(s)A(15). The 2 and G(1,6,7,8) determinants are also separated in inbred strains. The 2 determinant in inbred mice is not on the gammaF, gammaH, or gammaA heavy chain and is probably on a gammaG or gammaG-like immunoglobulin heavy chain. Papain digestion of serum from the Kyushu mouse showed two electrophoretically different Fc fragments, one carrying the G(1,6,7,8) and the other the 2 determinant. The new heavy chain allotype, (2)G(1,6,7,8)H(9,16)F(s)A(15), of the Kyushu wild mouse probably arose from a nonhomologous (unequal) cross over between (2)G(-)H(9,16)F(s)A(15) and G(1,6,7,8)H(9,11)F(f)A(12,13,14) heavy chain linkage groups. The linkage group of the Kyushu wild mouse has at least five heavy chain genes, while that of the inbred mice has four.

Animals↗
PubMed1968

Affinity site labeling of a mouse myeloma protein which binds dinitrophenyl ligands.

A mouse myeloma protein of the immunoglobulin A class, which specifically binds dinitrophenyl ligands, has been successfully affinity labeled (site-directed labeling) with several diazonium reagents, leading to inactivation of the combining sites. The labeling reagents reacted only with tyrosine residues of light chain origin. The 7S subunit of the myeloma protein appears to contain only one reactive site.

Animals↗
PubMed1968

Three IgA myeloma immunoglobulins from the BALB/ mouse: precipitation with pneumococcal C polysaccharide.

Three of 64 IgA immunoglobuilins, derived from plasma cell tumors induced by mineral oil in BALB/c mice, precipitated with species-specific pneumococcus C polysaccharide. A related antigen was also found in group O and some group H streptococci. A difference in ability to precipitate a C polysaccharide from a pneumococcus type XIV was demonstrated between protein 603 which did precipitate and protein 167 which did not precipitate this polysaccharide. Studies of the 167 and 603 proteins showed differences in electrophoretic mobility and polypeptide chains. The antigen-combining site of the 167 and 603 proteins resided on the papain-digestion Fab fragment.

Animals↗
PubMed1968

2-chain immunoglobulin A molecules: abnormal or normal intermediates in synthesis.

Immunoglobulin A (gammaA) myeloma proteins secreted by plasma-cell tumors of mice are of two types, a common four-chain molecule and a rare two-chain (3.9S) molecule. The close similarity between two-chain gammaA molecules and four-chain gammaA molecules and their polymers is demonstrated in tryptic peptide maps of isolated polypeptide chains and by precipitin reactions with rabbit antiserums to gammaA immzunoglobulins. However, a difference between these two types is distinguishable with homologous antiserums. Homologous antiserums to two-chain gammaA immunoglobulins are specific and do not cross-react with four-chain gammaA immutnoglobulins.

Animals↗