Antigenic and structural studies on human kappa Bence-Jones proteins.

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Further structural and antigenic studies of light-chain amyloid proteins. Scand J Immunol. Jul; 14 (1)– Solomon A.

Bence Jones proteins and light chains of immunoglobulins. XIV. Conformational dependency and molecular localization of the kappa (kappa) and lambda (lambda) antigenic determinants. Scand J Immunol. ; 5 ()–Cited by:   Aκ Bence Jones protein with phenotype Inv (1, −2) was isolated from the urine of a patient with multiple myeloma.

Inv typing of the patient's relatives established the presence of anInv 1 allele in the kindred, and that the patient's genotype wasInv 1/Inv 3.

Hence, the absence of Inv (2) in the Bence Jones protein was shown to be genetic and not an artifact caused by the by: By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S γ, β 2A, and β 2M.

All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or by: The epitope 3E10 is characteristic of 50% Bence Jones proteins of the II and III V lambda-subgroups thus representing a common idiotypic determinant.

Using anti-V lambda antibodies germ line variability of V lambda III proteins was analysed and the similarity of antigenic structure of normal and myeloma human Ig lambda chains was demonstrated.

Bence Jones proteins (23,24). E arlier it had been shown that the urinary Bence Jones proteins were the equivalent of the light chains of the myeloma protein in the blood of the same patient (25).

Th is observation of the variability in amino acid sequence in the N terminal residues of the human kappa. The effects of a number of chemical modifications on the expression of V κ and C κ antigenic determinants of a human kappa (subgroup I) Bence Jones protein was investigated.

Modification of ca. 88% of the ϵ-amino groups with citraconic anhydride or potassium cyanate was accompanied by decrease in C κ antigenicity with retention of complete idiotypic and subgroup by: 6.

a human lambda-type Bence-Jones dimer (molecular weight ); by Epp et al. [6] on the 8, map of the variable region of a human kappa-type Bence- Jones dimer (molecular weight 22 ) and by Padlan et al. [7] on the 8, map of the Fab fragment (molecular weight ) from the phosphorylcholineCited by: According to this hypothesis, study of the peptides of Bence-Jones proteins should facilitate the structural analysis of the normal and antibody y-globulins of man.

To this end we have thus far isolated and analyzed twelve of the tryptic peptides, designated B1 to B2o, from the Bence-Jones protein of antigenic Type 1, designated by: A new heavy chain disease protein ((gamma)HCD-JM) has been characterized by antigenic and structural criteria.

The protein belongs to the IgG3-subclass and is closely related to Fc-fragment of G3. Antigenic Structure, Function, and Evolution of the Hemagglutinin- Neuraminidase Protein of Human Parainfluenza Virus Type 1 Kelly J. Henrickson and Laura L. Savatski. STEIN S, NACHMAN RL, ENGLE RL. INDIVIDUAL AND SUB-GROUP ANTIGENIC SPECIFICITY OF BENCE-JONES PROTEIN.

Nature. Dec 21; – [Google Scholar] EPSTEIN WV, GROSS D. NATURALLY OCCURRING HUMAN ANTIBODY REACTING WITH BENCE JONES PROTEINS.

J Exp Med. Nov 1; – [Europe PMC free article] [Google Scholar]Cited by: ABS TRACT A new heavy chain disease protein (yHCD-JM) has been characterized by antigenic and structural criteria. The protein belongs to the IgG3-subclass and is closely related to Fc-fragment of G human Bence Jones proteins have been purified by gel filtration, digested with trypsin, and analyzed by peptide mapping.

In several cases Bence Jones "fragments", corresponding to the variable. G-myeloma protein (Daw)[1, 9, 10] was used as an antigen. In this paper the results of a study on the antigenic properties of this Fd-fragment will be described.

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MATERIALS AND METHODS The myeloma globulin (Daw) was a Gm (1), type L, 7S IgGl-protein. The. Primary structure of cryo Bence-Jones protein (TOG) from the urine of a patient with IgD myeloma.

Molecular Immunology16 (7), DOI: /(79) Bi-cheng Wang, Chung Soo Yoo, Martin Sax. Crystal structure of bence jones protein Rhe (3 Å) and its unique domain-domain by: The Bence Jones proteins from individual patients were found to correspond in antigenic group to that of the serum myeloma protein.

Studies with antisera to 7S γ-globulin and to Bence Jones proteins indicated that the Bence Jones proteins were antigenically identical to a portion of the corresponding multiple myeloma protein by: Immunoc%emistry. Pergamon Press Vol. 6, pp. Printed in Great Britain STUDIES ON THE ANTIGENIC PROPERTIES OF THE Fd-FRAGMENT OF A HUMAN G-MYELOMA PROTEIN (DAW) B.

ZEGERS and R. BALLIEUX Division of Immunochemistry, Department of Medicine, University Hospital, Utrecht, The Netherlands (First received 7 November ; in revised form 10 Cited by: 4.

the complete antigenic structure of the protein (see Atassi,for review). Human kappa Bence Jones proteins have been shown to express a large number of antigenic specifi- cities associated with variable (V~) sequences in addi- tion to the constant region (C~) determinants (Solo.

Further structural and antigenic studies of light-chain amyloid proteins. Scand J Immunol. Jul; 14 (1)– [Google Scholar] Solomon A. Bence Jones proteins and light chains of immunoglobulins. XIV. Conformational dependency and molecular localization of the kappa (kappa) and lambda (lambda) antigenic determinants.

Scand J Immunol. Bence-Jones proteins are urinary free light chains detected by urinary protein electrophoresis and immunofixation. From: Nephrology Secrets (Third Edition), Download as PDF.

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Bence Jones Proteins. Jean-Louis Preud'homme, in Encyclopedia of Immunology (Second Edition), Characterization. Guidelines for the Analysis of Bence Jones Protein Article (PDF Available) in Clinical Chemistry and Laboratory Medicine 41(3) April with 5, Reads How we measure 'reads'.

Cessation of corticosteroid therapy resulted in a prompt disappearance of the new protein and in a progressive increase in the amount of Bence Jones protein excreted. The new protein was isolated from the urine of this patient and was purified for comparative studies with Bence Jones protein and with the VL and CL prepared by specific enzymatic cleavage of the Bence Jones by: The ability of antiserum R to detect these antigenic differences on the intact immunoglobulin molecule, as well as on the isolated light chain or Bence Jones protein, made feasible the direct classification of type K myeloma proteins and M-macroglobulins (Waldenström).Cited by: Materials and Methods.-Bence-Jones proteins were initially isolated from urine by80%am-monium sulphate precipitation.

Proteins Ruand Ni were reprecipitated twice with 50% am-monium sulphate. Other proteins were further purified by DEAE-chromatography (phosphate buffer pH, gradient elution), Sephadex G gel filtration ( MTris-HCl buffer.

The three-dimensional structures of a Bence Jones protein and of Fab fragments from myeloma proteins established that the postulated domains are indeed spatially separated and share a common pattern of polypeptide chain folding, the Ig fold.

Since then, the introduction of myeloma hybridization techniques for the production of monoclonal antibodies and the impressive advances in molecular biology and biophysical techniques have greatly stimulated further biochemical and structural studies.

Ivanyi, J. Study of antigenic structure and inhibition of activity of human growth hormone and chorionic somatomammotropin by monoclonal antibodies.

Mol. Cited by: 9. Mannik M, Kunkel HG. CLASSIFICATION OF MYELOMA PROTEINS, BENCE JONES PROTEINS, AND MACROGLOBULINS INTO TWO GROUPS ON THE BASIS OF COMMON ANTIGENIC CHARACTERS.

J Exp Med. Nov 30; (6)– [Europe PMC free article] [Google Scholar]Cited by:   A comprehensive synthetic approach consisting of a series of consecutive, uniform overlapping peptides encompassing the entire protein chain was recently used to determine the full antigenic profile of the α-chain of human hemoglobin (Hb).

The peptides synthesized enabled the localization of five major “continuous” antigenic regions within the α by: Configurational antigenic specificity of γA-myeloma proteins, imposed by the presence of kappa L chains in native and appropriately recombined molecules, provides a further indication of the importance of noncovalent bonds in the establishment of the quaternary structure of these proteins Amino acid sequence studies with Bence Jones.

GENERAL FUNCTIONS OF IMMUNOGLOBULINS.

Description Antigenic and structural studies on human kappa Bence-Jones proteins. PDF

Antigen binding Immunoglobulins bind specifically to one or a few closely related antigens. Each immunoglobulin actually binds to a specific antigenic determinant. Antigen binding by antibodies is the primary function of antibodies and can result in protection of the host.

Atassi, M.Z., Precise determination of the entire antigenic structure of lysozyme: molecular features of protein antigenic structures and potential of “surface-simulation synthesis” -a powerful new concept for protein binding sites, Immunochem.

(). CrossRef Google ScholarCited by: - ratio of kappa to lambda light chains in human is - free light chains termed bence-jones proteins are found in the urine of pts with multiple myeloma.

- in general, antigenic determinants for antibody interactions are the most exposed (hydrophilic) regions of a molecule.Start studying Antibody Structure and Function Immunology Test and quiz #2. Learn vocabulary, terms, and more with flashcards, games, and other study tools.