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Tryptic peptides from the variable region of J558, xSl04, and S178 lambda chains 

Tryptic peptides from the variable region of J558, xSl04, and S178 lambda chains 

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Amino-acid sequences of the variable regions of three lambda chains produced by plasmacytomas of BALB/c mice are compared. Two are almost certainly identical and one differs from these by three amino acids. These findings extend our earlier conclusion on the relative uniformity of sequences in this type of immunoglobulin light chain. With amino-aci...

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Context 1
... 1 shows the tentative sequence of the variable region of the xS104, J558, and S178 lambda chains. The order of the variable-region tryptic peptides (Table 1) was established by certain chymotrypsin or thermolysin peptides isolated by electrophoresis and chromatography of digests of S-amino- ethylated lambda chains. The relevant peptides are the chymotrypsin peptides C-4, C-9, C-10, and C-20 (Table 2) and the thermolysin peptide Th-19 (Table 3). ...
Context 2
... to the NH2-terminal sequence of the first three residues of the T-2 peptide (Table 1) and could thus be placed at )position 24-34. The order of the thermolysin and the chymotrypsin peptides was established by their respective overlaps (Tables 2 and 3). ...
Context 3
... Arg2, Ala2, Pro2, Gly, Val, Phe) Thermolysin peptides used to establish the sequence and order of the tryptic peptides from the variable region of J558, xS104, and S178 lambda chains Tryptic peptide Peptide Residues Protein Amino-acid sequence Th-l 1-2 J558, xS104, S178 (Glx, Ala) ...

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... Furthermore, cDNA nucleotide sequence analysis of the entire variable and constant regions for the heavy and light chains of the L8D and 6-19J mAbs revealed a complete identity (data not shown) corresponding to the published nucleotide or amino acid sequences of the 6-19 ␥3 heavy chain and the J558 1 light chain. 11,27,42,43 This indicates that these 2 antibodies are identical in the amino acid sequences of their heavy and light chains Intraperitoneal implantation of L8D cells into (MRL ϫ BALB/ c)F1 mice induced a rapid increase in serum levels of IgG3 within 4 days (1.3 Ϯ 0.8 mg/mL), reaching 3 to 5 mg/mL at approximately 7 days. By day 10, all 8 mice developed severe acute glomerulonephritis similar to that induced by the original 6-19 RF hybridoma cells (Table 1, Figure 2A). ...
... Glycosylation of the IgG3 mAb studied should only occur in the constant region of their heavy chains because of the lack of potential glycosylation sites in their V H and V L regions. 11,42 Notably, in murine IgG3, there is an additional potential glycosylation site in its CH3 domain. 27 The presence of the CH3 oligosaccharides has been suggested by a recent demonstration that the self-associating ability was significantly reduced in a murine IgG3 RF mutant mAb lacking the glycosylation site in the CH3 domain. ...
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Chapter
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Chapter
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Chapter
Plasma cells are terminally differentiated cells of the B-cell lineage. They can develop from any of several mature B-cell subsets, including germinal center (GC), memory, marginal zone (MZ), and B1 cells. Plasma-cell tumors of mice, termed plasmacytomas (PCT), are increasingly recognized as sharing many features with the major type of plasma-cell tumors in humans, termed multiple myeloma (MM), an almost uniformly lethal disease. Consequently, an increasing number of mouse models of plasma-cell neoplasia are being developed to dissect the mechanisms underlying the initiation, progression, and maintenance of the transformed phenotype with the long-term goal of improving diagnosis and therapy. Studies of plasma-cell neoplasms in mice and humans have been remarkably informative for identifying genes and signaling pathways critical to normal B-cell differentiation, function, and survival, as well as neoplastic transformation (Fig. 24.1). Examinations of mouse plasma-cell neoplasms initiated in the National Cancer Institute over 50 years ago have been joined synergistically with studies in the National Institute of Allergy and Infectious Diseases, together with their collaborators, of normal and transformed plasma cells from retrovirus-infected and autoimmune mice. Together, they have painted an increasingly rich picture of the later stages of normal B-cell differentiation and the changes that redirect these cells to neoplasia. Other recent publications provide reviews of other plasma-cell tumor models, as well as other aspects of the studies described here [1,2].
Chapter
An immune serum usually consists of a very heterogeneous population of immunoglobulins (Ig’s) the appearance of which in the serum has been induced by antigen. The antigen-ligating function of the Ig molecule (see Figure 1) is confined to the combining regions, which are two symmetrical areas at the solvent-exposed ends of the Fab arms of the Y-shaped Ig molecules. The combining region is situated in the variable (V-region) domain, a compact region consisting of the N-terminal half of the light (L) chain and the N-terminal quarter of the heavy (H) chain that is linked by sulfhydryl bonds. Between the areas of this domain occupied by the L- and H-chain V regions is a cleft exposed to the solvent. Antigens have been shown to bind in, or close to, this cleft (Amzel et al., 1974). An induced antibody population is said to be specific because it usually binds most strongly to the immunizing antigen and with lesser binding energies to certain compounds that resemble the immunogen in structure. Heteroclitic antibodies may be induced that bind more strongly to some determinant other than the immunogen (Mäkelä, 1965). In general, antibody populations show a high degree of specificity, in that they are able to discriminate among chemical compounds differing by as little as a single functional group, between stereoisomers, or between two proteins differing by as little as a single amino acid residue (Reichlin, 1974).