Two families of monoclonal antibodies to alpha(1----6)dextran, VH19.1.2 and VH9.14.7, show distinct patterns of J kappa and JH minigene usage and amino acid substitutions in CDR3.

Nine groove-type mAb to alpha(1----6)dextran were cloned and sequenced. Together with previous reports from this laboratory, the VH and VL of 34 mAb have been sequenced, in which 10 VH19.1.

Amino acid substitutions in VH CDR2 change the idiotype but not the antigen-binding of monoclonal antibodies to alpha(1----6)dextrans.

An idiotype defined by mAb and polyclonal antibodies to 10.16.1, an anti-alpha(1----6) dextran was previously reported to be expressed on most BALB/c anti-alpha(1----6)dextrans with groove-type sites and to involved CDR3 and probably CDR2.

Immunochemical studies on the N-acetyllactosamine beta-(1----6)-linked trisaccharide specificity of Ricinus communis agglutinin.

The combining site of Ricinus communis agglutinin (RCA1) was studied by quantitative precipitin and precipitin inhibition assays. Of 31 complex carbohydrates tested, all except active and inactive antifreeze glycoproteins, Streptococcus group C polysaccharide, and native rat salivary glycoprotein, reacted strongly, and 22 completely precipitated the lectin, indicating that RCA1 has both a broad range of affinity and a low solubility of its carbohydrate-bound complex. Of the monosaccharides and glycosides tested for inhibition of precipitation, p-nitrophenyl beta-D-galactopyranoside was the best.

Different VL and VH germ-line genes are used to produce similar combining sites with specificity for alpha(1----6)dextrans.

Monoclonal antibodies to alpha(1----6)dextrans produced in mice immunized with the T-independent antigens alpha(1----6)dextran or the stearylisomaltosyl oligosaccharides have been characterized immunochemically. To correlate the immunochemical properties of these monoclonal antibodies with their primary structure, we have sequenced the variable (V) regions of the light (L) and heavy (H) chains. Three V kappa germ-line genes belonging to two major gene families were used; differential J usages also contribute to diversity.

Immunochemical studies of mouse monoclonal antibodies to dextran B1355S--II. Combining site specificity, sequence, idiotype and affinity.

The specificities of the combining sites of 19 mouse monoclonal antibodies to dextran B1355S have been characterized immunochemically by quantitative precipitin and precipitin inhibition assays; association constants for B1355S were determined by affinity gel electrophoresis. Cross-reactive and individual idiotypes related to the BALB/c B1355S-binding myeloma proteins MOPC104E [IdI(MOPC104E)] and J558 [IdI(J558)], determined by a radioimmunoassay, and heavy-chain variable-region sequences, are presented. Antibodies to B1355S are "alpha (1----3) alpha (1----6)-specific" as determined by precipitin and precipitin inhibition assays with dextrans and oligosaccharides, respectively, containing alternating alpha (1----3) alpha (1----6) linkages compared with oligosaccharides composed solely of alpha (1----3) or alpha (1----6) linkages; all antibodies have low association constants (less than or equal to 10(5) ml/g).

Immunochemical studies on blood groups. Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.

Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols. The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography. Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.