scholarly journals Dissociation of ϰ- and λ-chains from reduced human immunoglobulins

1965 ◽  
Vol 97 (2) ◽  
pp. 460-465 ◽  
Author(s):  
S Cohen ◽  
S Gordon
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Light Chain ◽  
Human Immunoglobulin ◽  
Light Chains ◽  
Type K ◽  
Human Immunoglobulins ◽  
Starch Gels ◽  
Bence Jones Proteins

1. The light chains of human immunoglobulin (Ig) exist in two forms, kappa (type K) and lambda (type L). The two types of chains can be partially separated by taking advantage of the fact that lambda-chains, for the most part, dissociate from reduced Ig at higher pH than do the kappa-chains. The same difference in dissociation of type K and L chains was observed with myeloma IgG and IgA proteins, but not with pathological IgM proteins. 2. When analysed in urea-glycine starch gels, pH7, both kappa- and lambda-chains show ten electrophoretic bands having the same mobilities as those of the whole light-chain subfractions. Normal kappa- and lambda-chains show similar differences in overall amino acid composition to those previously found with myeloma kappa- and lambda-chains and type K and L Bence-Jones proteins.

scholarly journals The stepwise removal of histones from chicken erythrocyte nucleoprotein

1968 ◽  
Vol 107 (2) ◽  
pp. 207-215 ◽  
Author(s):  
K. Murray ◽  
G. Vidali ◽  
J. M. Neelin
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chicken Erythrocyte ◽  
Histone Fraction ◽  
Buffer Solutions ◽  
Avian Erythrocytes ◽  
Zone Electrophoresis ◽  
Exclusion Chromatography ◽  
Starch Gels

1. A fractionation of chicken erythrocyte histones was achieved simultaneously with their extraction from saline-washed nuclei by stepwise titrations to progressively lower pH values. 2. Different acids and dilute buffer solutions of comparable pH behaved similarly in stepwise extractions of histones. 3. The histone preparations so obtained were characterized by their amino acid composition and behaviour on zone electrophoresis in starch gels. 4. The fractionation by titration was quite sharp at appropriate pH ranges, and the histone fraction that is apparently unique to avian erythrocytes was obtained without contamination by other histone fractions. 5. Histones prepared by stepwise titration were fractionated further by cation-exchange and exclusion chromatography. The chromatographic behaviour and amino acid composition of the components permitted comparison with histones prepared by other methods. 6. Histone fraction IIb was resolved into its subfractions IIb1 and IIb2 by exclusion chromatography on Bio-Gel P-60. 7. Histone fractions III and IV, previously reported to be absent from chicken erythrocyte nuclei, were found in extracts made at pH1.

Chemical structure of light chains: amino acid sequence of type K Bence-Jones proteins

1966 ◽  
Vol 166 (1003) ◽  
pp. 124-137 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Single Point ◽  
Structural Difference ◽  
Light Chains ◽  
Single Point Mutation ◽  
Amino Terminal ◽  
Type K ◽  
Bence Jones Proteins

Bence-Jones proteins are the light chains of the autologous myeloma globulin and are analogous to the light chains of normal human immunoglobulins. Peptide mapping has demonstrated that Bence-Jones proteins share a fixed portion of their sequence (the ‘constant’ portion) and also have a mutable part (the ‘variable’ portion). Sequence analysis and ordering of the tryptic and chymotryptic peptides has provided the tentative complete amino acid sequence of one Bence-Jones protein of antigenic type K. Comparison with partial sequence data for other type K Bence-Jones proteins has revealed many structural differences in the amino terminal half of the molecules, but only one structural difference in the carboxyl terminal half. The latter is strongly correlated with the Inv genetic factor. The points of interchange in the amino terminal half occur in clusters close to the half cystine residues and the ‘switch peptide’ (positions 102 through 105), after which the sequence becomes essentially invariant. This suggests that the major areas subject to sequence variation are part of a single topographical region which may define a portion of the antigen combining site in the light chains of antibodies. Many, but not all, the amino acid interchanges are compatible with a single point mutation. As yet, no single mutational theory suffices to explain the manifold differences in structure of the light chains. Such structural variation, however, could result from the presence of many related genes.

scholarly journals BENCE JONES PROTEINS AND LIGHT CHAINS OF IMMUNOGLOBULINS

1969 ◽  
Vol 130 (6) ◽  
pp. 1295-1311 ◽  
Author(s):  
Alan Solomon ◽  
Carla L. McLaughlin
Keyword(s):  
Light Chain ◽  
Light Chains ◽  
Bence Jones Protein ◽  
Amino Terminal ◽  
Type K ◽  
Myeloma Proteins ◽  
Immunoglobulin Molecule ◽  
Polypeptide Chains ◽  
Bence Jones Proteins

Three distinct classes of κ light polypeptide chains have been detected immunochemically by an antiserum (R185) prepared against a κ Bence Jones protein with a glutamyl amino terminal residue. This antiserum had specificity for κ light chains with glutamyl amino terminal residues and differentiated κ-chains with aspartyl amino terminal residues into two classes: the three κ-chain classes have been designated as κglu, κaspII, and κaspI. The ability of antiserum R185 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). The multispecificity of the antiserum permitted the quantitation of type κglu light chains in normal, hypergammaglobulinemic, and hypogammaglobulinemic sera. Whereas the distribution of myeloma proteins and Bence Jones proteins in the κglu class correlated with the distribution of κglu chains in normal and hypergammaglobulinemic sera, the M-macroglobulins in the κglu class represented 90% of the total M-macroglobulins tested and revealed a marked divergence from the range of 24–31% of κglu immunoglobulins in normal sera. A preponderance of κglu chains was detected in the sera from patients with non-sex-linked hypogammaglobulinemia and represented 60–77% of the total type K light chain content. The controlled cleavage of a Bence Jones protein representative of each κ-chain class into its variant half and constant half made possible the localization on the light polypeptide chain, the reactive sites for which antiserum R185 had specificity. The correlations between immunochemical and structural classification of κ light chains are discussed.

Antigenische Klassifizierung der Paraproteine und normalen Immunoglobuline vom Lambda-Typ / Paraproteins and Normal Immunoglobulins of the Lambda Type: Immunochemical Differentiation and Classification

1971 ◽  
Vol 26 (12) ◽  
pp. 1292-1302 ◽  
Author(s):  
F. W. Tischendorf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Basic Amino Acid ◽  
Light Chains ◽  
Antigenic Sites ◽  
Normal Individuals ◽  
Normal Light ◽  
Bence Jones Proteins

The elaboration of antisera recognizing antigenic sites of the variable region of pathological immunoglobulin λ chains (Bence-Jones-proteins) is described. The antisera react with the (St+) marker carried by Bence-Jones-proteins of the basic amino-acid sequence VλI and the (111+) marker carried by L-chains of the basic sequence VλIII. With these antisera three specificityregion subtypes of human λ immunoglobulin chains could be distinguished antigenically. Twenty randomly chosen normal individuals were shown to be associated with λ chains of both basic sequences, VλI and VλIII. The results provide evidence for the non-allelic nature of the two aminoterminal light chain forms (p<0.001) and suggest that the basic sequences VλI and VλIII of Bence-Jones-proteins represent two distinct subgroups of normal light chains.

Effect of maternal diet on the amino acid composition of human uterine fluid

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Maternal Diet ◽  
Uterine Fluid
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