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Biomedical subjects

M Potter

Publications and source records attributed to M Potter.

At least 325 records · Page 18Linked to original sources

Evidence for the linkage of the IGC H locus to a gene controlling the idiotypic specificity of anti-p-azophenylarsonate antibodies in strain A mice.

Anti-p-azophenylarsonate (anti-Ar) antibodies elicited in all strain A/J mice tested share one or more idiotypic specificities. These specificities are also found in the anti-Ar antibodies of mice of the closely related strain, AL/N, but not in those of BALB/c mice. Anti-Ar antibodies were elicited in congenic mice in which the IgC(H) locus of AL/N mice, which controls allotypic markers in the constant regions of heavy chains, had been introgressively backcrossed for nine generations onto a BALB/c background; the mice were then rendered homozygous for the AL/N allotypic determinant. On the average, these antibodies were quantitatively equivalent, with respect to content of the cross-reactive idiotype, to those of AL/N mice. This indicates that the gene controlling the idiotype is closely linked to the IgC(H) locus. Since idiotype must be a function of V region sequences, the results suggest close linkage of V(H) and C(H) genes. The cross-reactive idiotype was found in nearly all F(1) mice (C57/BL x A/J or BALB/c x A/J) tested.

Animals↗

Crystals of phosphorylcholine-binding Fab-fragments from mouse myeloma proteins: preparation and x-ray analysis.

Fab-fragments of several phosphorylcholine-binding mouse-myeloma proteins have been prepared by pepsin digestion; two of these, MOPC 167 and McPC 603, gave large crystals from ammonium sulfate solutions. The Fab-fragment from MOPC 167 crystallizes in a hexagonal space group, but does not diffract to a resolution greater than about 8 A. In contrast, McPC 603 crystals (space group P6(3)) diffract to about 2.7 A. An isotopic double-labeling technique was developed that demonstrated that the 603 crystals bind 1 mol of hapten per mol of Fab-fragment, but with a binding constant significantly lower than that observed in solution. The findings indicate that a three-dimensional model of this homogeneous antigen-binding immunoglobulin can be constructed. Accordingly, a search for heavy-atom derivatives and determination of the primary structure are in progress.

Animals↗

Synthesis, assembly, and secretion of gamma globulin by mouse myeloma cells. 3. Assembly of the three subclasses of IgG.

The synthesis, assembly, and secretion of the three major subclasses of mouse IgG has been examined in 14 myeloma tumors and two cultured cell lines as well as in the cells from the popliteal lymph nodes of immunized mice. The total amount of IgG synthesized was between 15 and 43% of the cytoplasmic proteins made during a 15 min period. H(2) and H(2)L were the major precursors of IgG(2a) and IgG(1) but, in all of the tumors, HL was also an intermediate. In contrast, HL was a major precursor of IgG(2b). Most of the noncovalent and covalent assembly of IgG occurred after release of the newly synthesized H and L chains from the polyribosomes and assembly was not completed until 10 min or more after the synthesis of the polypeptide chains.

Animals↗