scholarly journals AN IDIOTYPIC CROSS-REACTION BETWEEN ALLOTYPE a3 AND ALLOTYPE a NEGATIVE RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATE

1973 ◽  
Vol 137 (3) ◽  
pp. 636-648 ◽  
Author(s):  
Thomas J. Kindt ◽  
David G. Klapper ◽  
Michael D. Waterfield
Keyword(s):  
Chemical Analysis ◽  
Cross Reaction ◽  
The Other ◽  
Light Chains ◽  
Binding Affinities ◽  
Variable Regions ◽  
Heavy Chains ◽  
Relative Binding ◽  
Group A

Two antibodies to Group C streptococcal carbohydrate isolated from an individual rabbit had similar relative binding affinities for a Group C immuno-adsorbent column. Their light chains were similar, if not identical, as were the constant regions of their heavy chains. Differences in the variable regions of the H chains of the two antibodies were detected by chemical analysis. The two antibodies had serologically identical idiotypic determinants although one antibody possessed the a3 allotype and the other had no detectable group a marker. The occurrence of such antibodies indicates the absence of obligatory associations between group a allotypes and idiotypic specificities, despite the fact that both determinants have antigenic components in the VH region of the H chain.

Genetic control of immunoglobulin synthesis

1970 ◽  
Vol 176 (1044) ◽  
pp. 329-346 ◽  
Keyword(s):  
Genetic Control ◽  
Mammalian Species ◽  
Variable Region ◽  
Lymphoid Cells ◽  
The Other ◽  
Light Chains ◽  
Common Region ◽  
Variable Regions ◽  
Immunoglobulin Synthesis ◽  
Heavy Chains

The structural features of immunoglobulins are described. This family of related proteins shows a common structural design: two identical light chains and two identical heavy chains are present in each molecule. Amino acid sequence studies have shown that light chains have one of two types of sequences in the C terminal half, whereas they differ one from the other in the N terminal half. The two halves of the sequence have been designated accordingly variable and common half. Similarly, the heavy chains have a common sequence in the C terminal three-quarters of the sequence and a variable one in the N terminal quarter. Genetic studies on the inheritance of immunoglobulin alleles have been carried out in some mammalian species. The genetic control of immunoglobulin synthesis is reviewed in man, mouse and rabbit. These studies have shown that each allele controls the inheritance of a specific common region, with the exception of one genetic system which seems to control the synthesis of the variable region of rabbit heavy chains. Immunoglobulin chains are clearly synthesized under the control of two distinct genetic elements, one of which specifies the variable region and the other the common region. The possible significance of this type of genetic control of immunoglobulin structure is discussed. It has not yet been established whether each variant of the variable region is coded for by an individual structural gene present in the genome of each individual or whether few genes for variable regions exist, which in the course of the differentiation of lymphoid cells are subject to somatic mutation processes, which generate variability. These two possibilities are discussed and elements in favour of one or the other theory are presented.

scholarly journals Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment

1968 ◽  
Vol 106 (1) ◽  
pp. 15-21 ◽  
Author(s):  
B. Frangione ◽  
C. Milstein ◽  
Edward C. Franklin
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
The Other ◽  
Light Chains ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Other Hand ◽  
Terminal Loop ◽  
Heavy Chain Disease

The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present. The sequences appear to be identical in the Fc fragments of two types of chain studied (γ1 and γ3), and very similar to corresponding sequences of the Fc fragment in rabbit. These results suggest that the C-terminal half of the heavy chains is covalently folded (in a similar fashion to the light chains) with a C-terminal loop and an N-terminal loop. The similarity is emphasized by comparison of the sequence and location of the disulphide-bridged peptides of the C-terminal loop of heavy and light chains. The N-terminal loop, on the other hand, appears to be very different in Fc fragments and light chains. The C-terminal loop is the only one present in the F′c fragment.

scholarly journals Expression of a public idiotype by human monoclonal IgM directed to myelin-associated glycoprotein and characterization of the variability subgroup of their heavy and light chains.

1989 ◽  
Vol 170 (5) ◽  
pp. 1551-1558 ◽  
Author(s):  
J C Brouet ◽  
K Dellagi ◽  
M C Gendron ◽  
A Chevalier ◽  
C Schmitt ◽  
...  
Keyword(s):  
Nonhuman Primate ◽  
Light Chains ◽  
Antibody Activity ◽  
Rheumatoid Factors ◽  
Variable Regions ◽  
Cold Agglutinins ◽  
Heavy Chains ◽  
Myelin Associated Glycoprotein ◽  
Kappa Light Chains

Most studies using rabbit or mouse antisera failed to detect CRI between human IgM directed to MAG. We show here that 9 of 10 such IgM express a public CRI as defined by a nonhuman primate antiserum. Shared idiotype is likely involved in (or close to) the combining site of those IgM since antiidiotypic serum inhibited the binding of IgM to MAG and reacted with IgM having different variable regions of light and heavy chains. Partial aminoterminal sequence of heavy and light chains showed that anti-MAG IgM use either lambda chains (one IgM) or kappa light chains (six IgM) of different variability subgroups (V kappa IV in three instances, V kappa I in two, and V kappa II in one), whereas heavy chains belong to the VHIII (six IgM) or to the VHII (1 IgM) subgroup. These features distinguish these IgM from other human monoclonal IgM with a defined antibody activity, such as rheumatoid factors or cold agglutinins.

scholarly journals The amino acid sequences of the Fd fragments of two human γ 1 heavy chains

1970 ◽  
Vol 117 (4) ◽  
pp. 641-660 ◽  
Author(s):  
E. M. Press ◽  
N. M. Hogg
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Heavy Chain ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Aspartic Acid Residue ◽  
Variable Regions ◽  
Heavy Chain Variable Region ◽  
Heavy Chains

The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another γ 1 chain, Eu, a μ chain, Ou, and the partial sequence of a fourth γ 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the γ 1 chains, Cor.

An Atypical Human Immunoglobulin G with Deletions in both Heavy and Light Chains. Studies of the Conformation and the In Vitro Recombination of the Isolated Subunits

1974 ◽  
Vol 52 (7) ◽  
pp. 610-619 ◽  
Author(s):  
M. E. Percy ◽  
K. J. Dorrington
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Hypervariable Region ◽  
Light Chains ◽  
Constant Region ◽  
Myeloma Protein ◽  
Variable Regions ◽  
Heavy Chains ◽  
Amino Terminal

Both the light and gamma (heavy) chains of IgG(Sac) contain extensive deletions in their variable regions. The deletion in the light chain is internal (residues 18–88), whereas the deletion in the heavy chain is amino-terminal (residues 1–102). The hypervariable region just preceding the beginning of the constant region in other heavy chains (residues 103–115) is amino-terminal in heavy chain(Sac). In 4 mM acetate, pH 5.4, heavy chain(Sac) is dimeric like normal gamma chains, whereas light chain(Sac) is monomeric. Isolated light and heavy chains of IgG(Sac) recombine in vitro with each other and also with the heavy and light chains from a typical human IgG1-K myeloma protein, but not in a fashion entirely typical of other human gamma and light chains. These studies support the concept that non-covalent forces between the variable regions of the light and heavy chains are important in the assembly of the immunoglobulin molecule; and in view of the weak interaction between the constant region of light chain and heavy chain observed previously, our data suggest that there are points of contact between the hypervariable region of the gamma chain (residues 103–115) and the variable region of the light chain.

scholarly journals Epitopes of streptococcal M proteins shared with cardiac myosin.

1985 ◽  
Vol 162 (2) ◽  
pp. 583-591 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Acute Rheumatic Fever ◽  
M Protein ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Poststreptococcal Glomerulonephritis ◽  
Heavy Chains ◽  
M Proteins ◽  
Group A

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.

scholarly journals SIX BALB/c IgA MYELOMA PROTEINS THAT BIND ß-(1 → 6)-D-GALACTAN

1973 ◽  
Vol 138 (5) ◽  
pp. 1095-1106 ◽  
Author(s):  
Stuart Rudikoff ◽  
Elizabeth B. Mushinski ◽  
Michael Potter ◽  
C. P. J. Glaudemans ◽  
Michael E. Jolley
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Heavy Chain ◽  
Antigenic Determinant ◽  
Amino Acid Sequences ◽  
The Other ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Highly Sensitive

Six IgA myeloma proteins of BALB/c origin which bind antigens containing ß-(1 → 6)-D-galactan side chains have been isolated by affinity chromatography on galactoside-BSA-Sepharose columns. Partial amino acid sequences of of the light chains to residue Cys23 and the heavy chains to reside 30 were determined on the automated sequencer. No differences were found among the six VK sequences. Among some 50 partial VK sequences that have thus far been determined these six chains are the only ones thus far identified in this subgroup; at least 25 VK subgroups in the mouse have been identified so far. The heavy chain partial sequences were also very closely related but two differences were found. One protein differed from the other five by having isoleucine instead of leucine at position 5, a second protein differed from the others by having an unidentified amino acid at position 19. Using the highly sensitive inhibition of hemagglutination method it was found that each of the proteins possessed a unique inidividual antigenic determinant.

scholarly journals INDEPENDENT SYNTHESIS OF LIGHT AND HEAVY CHAINS

1974 ◽  
Vol 140 (4) ◽  
pp. 1112-1116 ◽  
Author(s):  
Reuven Laskov ◽  
Matthew D. Scharff
Keyword(s):  
Tissue Culture ◽  
Cell Line ◽  
Cell Lines ◽  
Light Chain ◽  
The Other ◽  
Light Chains ◽  
Parent Cell ◽  
Intracellular Pool ◽  
Heavy Chains ◽  
Independent Synthesis

The rates of immunoglobulin synthesis have been examined in two MFC-11 cell lines which were independently adapted to tissue culture and in light-chain-producing variants derived from each of them. One cell line synthesized 2.5 pg immunoglobulin/cell/h, while the other synthesized 3.6 pg immunoglobulin/cell/h. The ratio of heavy and light chains in the two cell lines was approximately the same, and the size of the intracellular pool of immunoglobulin was proportioned to the rate of synthesis. Variants which had spontaneously lost the ability to produce heavy chains continued to synthesize light chains at approximately the same rate as their parent cell line.

Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography

1988 ◽  
Vol 46 ◽  
pp. 156-157
Author(s):  
Donald A. Winkelmann
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Actin Filaments ◽  
Light Chains ◽  
Myosin Filament ◽  
Primary Role ◽  
Heavy Chains ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Globular Head

The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globular head that binds actin and hydrolyses ATP. Myosin can be fragmented by limited proteolysis into several structural and functional domains. It has recently been demonstrated using an in vitro movement assay that the globular head domain, subfragment-1, is sufficient to cause sliding movement of actin filaments.The discovery of conditions for crystallization of the myosin subfragment-1 (S1) has led to a systematic analysis of S1 structure by x-ray crystallography and electron microscopy. Image analysis of electron micrographs of thin sections of small S1 crystals has been used to determine the structure of S1 in the crystal lattice.

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