Bence-Jones proteins and light chains of immunoglobulins (first of two parts).
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Alleles↗
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Results for “Immunoglobulin lambda-Chains”
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Detection of small numbers of monoclonal B lymphocytes in the blood of patients with lymphoma.
The definition of complete remission and early relapse in patients with lymphoid malignancy is complicated by the difficulty of recognizing the presence of small numbers of malignant lymphocytes in a population of normal lymphocytes. We have used a method based on the cytofluorometric detection of lymphocytes having homogeneous amounts of surface immunoglobulin of one light-chain class to study blood from patients with lymphomas. The test is capable of reliably detecting 10 per cent or less of monoclonal B lymphocytes in normal blood, and it shows a high incidnece (30 to 40 per cent) of previously unsuspected monoclonal B lymphocytes in patients who were though to have no abnormal blood cells according to standard morphologic technics. The ability to estimate the number of such cells may facilitate the planning of therapy and make more meaningful the concept of complete remission.
Adult↗
Seek well and ye shall find.
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B-Lymphocytes↗
Structure and specificity of antibody molecules.
The structure of the Fab' fragment of a human myeloma protein (IgG1 (lambda) New) has been determined by X-ray crystallographic analysis to a nominal resolution of 0.2 nm. Each of the structure subunits corresponding to the variable and to the constant homology regions of the light and heavy polypeptide chains contains two irregular beta-sheets which are roughly parallel to each other and surround a tighly packed interior of hydrophobic side chains. The regions of the hypervariable sequences in the light and heavy chains occur in close spatial proximity at one end of the molecule, defining the active site of IgG New. The role of these hypervariable regions in defining the size and shape of the active site of different immunoglobulins is discussed on the basis of the three-dimensional model of Fab' New. Several ligands that bind to the active centre of IgG New have been used to obtain crystalline ligand-Fab' New complexes which were investigated by difference Fourier maps. These studies are analysed in terms of the biological function and specificity of antibodies.
Amino Acid Sequence↗
Contamination of anti-immunoglobulin reagents with antibodies to beta 2-microglobulin and other unrelated antigens. Effects on immunofluorescence staining of human lymphocytes.
IgG fractions from three of four rabbit antisera to Bence Jones proteins of chi-type were found to contain antibodies to beta 2-microglobulin and to stain 80%-100% of human blood lymphocytes by indirect immunofluorescence. Antibody fractions from these sera, which contained anti-beta 2-microglobulin but not anti-Ig, stained all lymphocytes, whereas the isolated anti-Ig antibodies (anti-chi) stained only a minor cell population. In both instances, the specificity of the staining was confirmed by absorption experiments. One antiserum to the constant half of lambda-type Bence Jones protein also contained antibiodies to beta 2-microglobulin and stained all lymphocytes. Four other anti-lambda reagents contained no antibodies to beta 2-microglobulin and stained at most about half of the lymphocytes. The antigen responsible for this staining is unknown. The isolated anti-immunoglobulin antibodies (anti-lambda) stained only 5%-10% of the lymphocytes. Antisera to serum IgG or its fragments were free of antibodies to beta 2-microglobulin and stained only 10%-25% of the lymphocytes. This staining was in all instances due to antibodies to human immunoglobulin. Five of eight undiluted sera from normal rabbits with no detectable antibodies to human immunoglobulin or beta 2-microglobulin stained 25%-60% of the lymphocytes. This staining rapidly disappeared on dilution.
Antibodies↗
Coexistence of protein AA and immunoglobulin light-chain fragments in amyloid fibrils.
Coexistence of amyloid fibril protein AA and homogeneous immunoglobulin light-chain fragments was found in the isolated amyloid fibrils of two patients with amyloidosis secondary to rheumatoid arthritis. The light-chain amyloid fibril protein showed antigenic identity with a light-chain amyloid from a patient with primary amyloidosis, which was identified as the VlambdaIV subgroup by amino acid sequence analysis. In the amyloid fibrils isolated from another patient with primary amyloidosis there was a mixture of VlambdaIV and VlambdaV homogeneous immunoglobulin light chains. Thus, a mixture of protein AA had lambda light chains or two different types of homogeneous light chains may be found in the amyloid fibrils of some patients.
Amino Acid Sequence↗
Bence Jones proteins and light chains of immunoglobulins. XIV. Conformational dependency and molecular localization of the kappa (kappa) and lambda (lambda) antigenic determinants.
The region on the light chain molecule responsible for expression of the kappa and lambda antigenic determinants was determined by comparative immunochemical analyses of intact Bence Jones proteins and naturally occurring or enzymatically derived fragments of Bence Jones proteins that lacked extensive portions of the V region or part of the C region. The reactivity of these fragments with numerous antisera having specificity for light-chain antigenic determinants indicated the essentiality of the intact light polypeptide chain for expression of the kappa and lambda antigenic determinants. The conformational dependency of the kappa and lambda antigenic determinants was also evidenced by denaturation-renaturation studies on kappa and lambda chains. The V domain, C domain, and interdomain 'switch' region contribute to the expression of kappa and lambda antigenicity and to certain isotypic and allotypic specificities.
Amino Acid Sequence↗
Characterization of IgD. I. Isolation of two molecular forms from human serum.
Human IgD present in the serum of normal individuals or of patients with Hodgkin's disease (having high IgD concentrations) was characterized and compared with five IgD myeloma proteins. IgD was isolated using a highly specific anti-delta insoluble immunoabsorbent from which the bound material was eluted with sodium dodecyl sulphate (SDS) or urea. The latter reagent could be removed by extensive dialysis, thus making possible the renaturation of the eluted molecules. The purity of the IgD thus isolated was confirmed by antigenic analysis. Both kappa and lambda light chain determinants were present on serum IgD, although lambda light chain was predominant with a ratio over the kappa chain of 2:1. SDS-polyacrylamide slab gel electrophoresis analysis revealed two different molecular forms of serum IgD, one (IgD) migrating identically to monoclonal IgD, the other (IgD2) having a faster mobility. The difference between the two molecules was entirely, due to the different sizes of their constituent delta chains. Peptide mapping of the two chains (delta1 and delta2 respectively) and of the delta chain of an IgD myeloma protein was carried out using 125I-labelled material. The three molecules displayed a high degree of homology, the delta2 chain differing by the presence of three characteristic extra peptides. The significance of these extra peptides is discussed in the light of the peptide mapping technique employed.
Autoradiography↗
Demonstration of oligoclonal immunoglobulin G IN Guillain-Barré syndrome.
Elevated concentrations in CSF of the immunoglobulins G, A, and M, when expressed as a percentage of the total protein concentration of CSF, were demonstrated during the initial phase of the course of the disease in a patient with Guillain-Barre syndrome (GBS). A slight elevation of the relative concentrations of IgG and IGM in CSF were also registered later in the course of the disease, at the time when the patient's neurological symptoms were in regression. Multiple discrete IgG bands were demonstrated by agarose electrophoresis in serum and in CSF during the first 2 weeks after onset of the neurological symptoms, and also after week 2 and still during week 12 after onset. The finding of transient oligoclonal IgG in a parient with GBS may suggest stimulation with e.g. viral antigen.
Blood Proteins↗
Cellular immunity to encephalitogenic protein in multiple sclerosis. Correlations with other laboratory characteristics at different disease courses.
A very suggestive, although non-significant, correlation was found between cellular immunity to encephalitogenic protein in multiple sclerosis and the genetic marker HLA-B7 in patients with no disease activity during at least the past 5 years and in those with a chronic progressive disease course during recent years, but not in patients studied longitudinally after a relapse. Only the latter group showed a significant correlation with parameters indicating intrathecal synthesis of immunoglobulin. No correlation was demonstrable with a parameter indicating intrathecal synthesis of measles antibodies.
Antibodies, Viral↗
Immunoglobulin diversity: correlation of non-allelic antigenic markers with the basic sequences of the variable region of human lambda chains.
Three forms of the amino terminal half (variable region) of human pathological lambda light chains of immunolglobulins were identified antigenically. By study of all completely sequenced Bence Jones proteins hitherto analyzed and a greater number of proteins subjected to automated sequence determination as well as normal light chains three distinct isotypic basic sequences were identified. The basic sequences are shown to be associated with characteristic antigenic markers representing three V region genes encoding the variable half of lambda chains of immunoglobulins.
Alleles↗
Isolation of a VHClambda fragment on tryptic digestion of human IgD myeloma proteins.
The tryptic digestion pattern of IgD myeloma proteins is reported. The Fab delta of fragment is shown to be very susceptible to further degradation to yield a novel fragment composed of VH and Clambda domains which are still bound through the interchain disulphide bridge. Reduction results in a change in M.W. from ca. 26,000 to 13,000. The loss of Fd delta of isotypic determinants may be of importance to studies in which membrane bound IgD is detected or measured after release from the cell surface by enzyme digestion.
Epitopes↗
[Comparative study of a factor-VIII inhibitor in a non-hemophylic patient and in a patient with hemophylia A gravis].
In this study, we tried to make a comparison between the findings concerning two human strong anti Factor VIII inhibitors. In one case, the strong inhibitor appeared in an old man without any particular antecedant. In the second case, it occurred in a young hemophiliac A. We found in both cases that the inhibitor was a immunoglobulin G with light chain lambda. Its activity site is on the fragment AB. These anticoagulants have a inhibitory action against only the Factor VIII procoagulant fraction and have exclusively neutralising properties. The inhibitor present in the non hemophiliac patient has particularly great resistance to temperature and pH variations.
Adult↗
Monoclonal IgG1 immunoglobulinaemia with strictly pH dependent cryoprecipitability.
A monoclonal IgG1 lambda protein with peculiar cryoprecipitable characteristics was found in the serum of a patient with advanced multiple myeloma. The cryoprecipitate was observed only when the serum was exposed to the air. Further studies defined this phenomenon as being strictly pH-dependent. No antiglobulin activity (rheumatoid factor) was detected in the cryoglobulin. The isoelctric focussing of isolated cryoglobulin showed four distinct fractions around the pH 7.8 zone, which was comparable to the pH at which the cryoprecipitate began to form. Electrostatic bonds probably contribute to the mechanism involved in the formation of cryoprecipitate in this case.
Aged↗
Structural studies of the Xenopus 19S immunoglobulin and 7S immunoglobulin and two immunoglobulin-like proteins.
Xenopus laevis 19S and 7S immunoglobulins (Ig) were extensively reduced and alkylated, their H and L chains spearated and their molecular weights determined. Two kinds of L chains of molecular weight 25,000 and 27,000 were revealed by SDS-polyacrylamide gel electrophoresis. In addition two Ig-like proteins consisting of heavy chains only, of 19S H-type and with similar molecular weight, were detected in Xenopus serum ans isolated. These proteins share common antigenic determinants with Xenopus 19S Ig heavy chains and are devoid of light chain determinants.
Alkylation↗
[Ratio of light kappa to lambda chains in monoclonal non-reticuloma protein].
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Adult↗
Heterogeneity of human circulating anticoagulants against antihemophilic factor (factor VIII).
The heterogeneity of human circulating anticoagulants against antihemophilic factor (AHF, factor VIII) observed in seven patients, both with and without classic hemophilia, was investigated by neutralization of their activity with antiserums directed to whole IgG and to lambda and kappa light chains. All seven anticoagulants were immunoglobulins. Six appeared to contain both kinds of light chains, although the dual light chain composition of two of these could be demonstrated only at high concentration of antiserum. In one circulating anticoagulant, light chain specificity could not be demonstrated with small amounts of antiserum, and with larger amounts, only lambda light chain specificity was revealed. Whether or not this circulating anticoagulant really contained a single light chain type could not be ascertained with our technique. The evidence presented suggested that circulating anticoagulant antibodies against AHF are polyclonal in nature.
Absorption↗
The association of alpha2-macroglobulin with lymphocyte membranes in chronic lymphocytic leukaemia and other disorders.
The association of alpha2-macroglobulin (alpha2M) with the surface membranes of human peripheral blood lymphocyte preparations has been investigated by the direct immunofluorescent technique. The percentage (and total number) of lymphocytes with detectable alpha2M on their surface is significantly increased in chronic lymphocytic leukaemia. The incidence of alpha2M-positive cells in normal and pathological conditions closely parallels that observed with conjugated antiserum to the kamma and gamma light chains of human immunoglobulin. It bears no relationship however to the plasma alpha2M levels or to the age of the donor. Additional blocking studies with aggregated human IgG, soluble antigen-antibody complexes and the F(ab')2 moiety of the anti-alpha2M, and indirect immunofluorescent studies with the latter, indicate that the fluorescence observed is not due to interaction of the conjugated reagent with Fc or C3 receptors.
Adult↗