Immunoglobulins chain

The residues not in the framework region form the loops between the p strands. These loops may vary in length and sequence among immunoglobulin chains of different classes but are constant within each class the sequence of the loops is invariant. The functions of these loops are not known, but they are probably involved in the effector functions of antibodies. When an antibody-antigen complex has been formed, signals are... 

Ein, D. (1968). Nonallelic behavior of the Oz groups in human lambda immunoglobulin chains. Proc. Natl. Acad. Sci. USA 60,982-985. 

Figure 4. SDS-PAGE profile of monoclonal antibodies HSA-1 and HSA-2. After purification by hydroxyapatite chromatography, HSA-1 (lane 2) and HSA-2 (lane 3) were electrophoresed on a 10% polyacrylamide gel in the presence of 0.1% SDS. Approximately 1 (xg of HSA-1 and HSA-2 was loaded in each lane. The gel shows two peptide bands corresponding to heavy and light (56-and 24-kilodalton [KD], respectively) immunoglobulin chains and no evidence of other contaminating proteins. Lane 1 was loaded with molecular weight markers.

Haas, 1. G. (1991). BiP—A heat shock protein involved in immunoglobulin chain assembly. Curr. Top. Microbiol. Immunol. 167, 71-82. 

Another serious problem is the tendency to select for sequencing immunoglobulin chains in which the amino terminus is unblocked because of the ability to use the sequencer. This too is skewing the data base so that answers to many questions cannot be obtained. Pyroglutamic acid (pyrrolidonecarboxylic acid) was present at the amino terminus in 18/21 human VHI, 5/6 VHH, and 5/5 VHIV chains sequenced as well as in 10/10 human VXI, 16/20 VxII, 3/3 V V, 19/19 mouse Vx chains and in the 1 pig Vx chain sequenced (Kabat et al., 1976b). 

VI. Correlation of Variability with Physicochemical Properties of Amino Acids in Immunoglobulin Chains... 

Rabat, E. A., Wu, T. T., and Bilofsky, H. (1976b). Variable Regions of Immunoglobulin Chains. Medical Computer Systems, Bolt, Beranek Newman, Cambridge, Massachusetts. 

Immunoglobulin (Ig) light chains are responsible for quite a few protein deposition diseases. Some immunoglobulin chains form amyloid deposits, whereas others do not. A protein conformational change in the partially folded protein is involved that subsequently leads to association and fibril formation. During the folding pathway of especially larger proteins, hydrophobic patches may be exposed. ... 

Vine ND, Drake P, Hiatt A, et al. Assembly and plasma membrane targeting of recombinant immunoglobulin chains in plants with a murine immunoglobulin transmembrane sequence. Plant Mol. Biol., 2001 45(2) 159-167. 

Fig. 10. Domain composition of immunoglobulin chains. Membrane-bound immunoglobulins have ex tra C-terminal segments. IgD composition is that of human IgD mouse IgD lacks the C,2 domain.

Fig. 8. Regulation of immunoglobulin chain expression. The expression of an immunoglobulin chain after productive VH to DJM or VL to J, rearrangement is indicated by a solid line. The regulatory influence of the IgH chain or the complete immunoglobulin molecule is indicated by a dashed line.

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