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BIOCHEMICAL CHARACTERIZATION OF SEROLOGICALLY-DEFINED RABBIT HEAVY CHAIN VARIABLE REGION ALLOTYPES OF THE A AND Y SUBGROUPS (IMMUNOGLOBULIN, IDIOTYPE, PEPTIDE MAPPING)

Structural studies on the serologically-defined rabbit VHa('+) (a1, a2, and a3) and VHa('-) (y33,30 and y33,-) immunoglobulins have been performed in order to establish that these genetic markers reflect the presence of different primary gene products. In addition, biochemical studies were carried out on induced non-a2 anti-a1-reactive molecule in order to determine whether these molecules represent latent allotypes or are an internal image idiotype. / Initially, allotype-defined heavy chains were prepared from the affinity-purified IgG molecules. These were then subjected to tryptic digestion and were analyzed by HPLC. Approximately 38-40 distinct peptides were resolved from each heavy chain, of which about 30 peptides were derived from Fc fragment (CH2 and CH3) and 8-10 peptides were derived from Fd region (VH1 and CH1). Seven Fd peptides were shared by all VHa('+) and VHa('-) heavy chains. Each of the a1 and the a2 digests had one allotype-specific peptide (in addition to the common peptides), whereas no allotype-specific peptides were observed for a3 heavy chain. No differences were detected between y33,30 and y33,- peptides, however, both expressed a common y-specific peptide. / Comparison of the nominal a1 digest with non-a2 anti-al-reactive heavy chain digest revealed that non-a2 anti-a1-reactive molecule expressed an a1-specific peptide. This observation, together with previous immunoelectron microscopic data, suggests that non-a2 anti-a1-reactive molecule are possibly latent a1 allotype. / Amino acid analyses of the isolated a1 and y-specific peptides indicate that the y-specific peptide is very similar to the first 19 N-terminal amino acid residues of the previously reported pooled VHa('-) molecule (e.g., the two peptides matched at 16 residues out of 19 residues). The a1-specific peptide was very similar (except one extra amino acid) to the N-terminal 10 amino acid residues of the VHa1 molecule. These data indicate that both a1 and y-specific peptides are located in the first VH framework region. / Source: Dissertation Abstracts International, Volume: 46-01, Section: B, page: 0052. / Thesis (Ph.D.)--The Florida State University, 1984.

Identiferoai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_75498
ContributorsABOLHASSANI, MOHSEN., Florida State University
Source SetsFlorida State University
Detected LanguageEnglish
TypeText
Format166 p.
RightsOn campus use only.
RelationDissertation Abstracts International

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