Myeloma globulin

Figure 1 shows diagrammatically the arrangement of the proteins of the serum in accordance with their mobilities, as would be found in a classical electrophoretical pattern obtained by electrophoresis of normal serum at pH 8.6 in veronal buffer. The Bence-Jones and myeloma globulins are also placed in areas where they were found in respect to the serum proteins indicated (see Table V for other data on these proteins). In each system, in both the hepatic and extrahepatic proteins (26), the ala-thr ratios change in the same direction as the... 

Idiotypic specificity—Antibodies and myeloma globulins of a given specificity show differences in antigenic specificity ascribable to differences in sequence in the variable regions of their light and heavy chains. Some of these idiotypic determinants are inhibitable by the antigenic determinant or ligand for which the antibody or myeloma protein is specific, whereas others are not. Those idiotypic determinants which are inhibitable are hypothesized to in-... 

The same investigators studied the antigenic relationship between purified Bence Jones uroproteins, multiple myeloma globulins, and normal y-globulin. All 18 Bence Jones proteins cross-reacted with anti-y-globulin sera they showed mobilities between 1.4 and 4.7 cm volt sec X 10 and S2o-values from 2.14 to 4.60. Bence Jones proteins were found to be antigenically more deficient than either myeloma globulins... 

The antibodies are similar in structure to other globulin proteins which are present in serum of vertebrates [9], The antibody molecule consists of two light polypeptide chains and two heavy polypeptide chains [10]. The amino acids are present in all the chains but the number of residues and the sequence will vary in different antibody multiforms [9], Light chains contain approximately 220 amino add residues and heavy chains about 450 residues. The complete sequence of the chains of human IgG myeloma protein has been determined by Edelman [11], The chains are held together in the unique conformational structure of the antibody molecule by a few covalent disulfide bonds between the chains and many electrostatic bonds between the amino groups of one chain and the hydroxyl groups of another chain. The covalent bonds are represented in Formula 1, 2 and 3 [peptide, disulfide and... 

The remarkable similarity in the molar ratios of the amino acids offers encouragement to the proposition that common peptides will be found in the electrophoretic components of the serum proteins. The peptide of spot 7 probably differs from spot 8 in leucine content, which would account for the higher Rf of spot 8. More encouraging are the recent reports of Edelman (2, 13) who found that gamma-globulin, the Bence-Jones proteins, and the myeloma proteins have a peptide unit of common amino acid composition. 

Monoclonal immunoglobulin has been used as a marker for multiple myeloma for more than 100 years.Monoclonal paraproteins appear as sharp bands in the globulin area of the serum electrophoretic patterns. More than 95% of... 

The serum albumin of cancer patients also appears to bind less PSP than normal. This is thought (B18) to be due to the occupation of PSP-binding sites by unknown substances occurring in the blood in cancerous states, since after isolation and treatment with alcohol, but not after exhaustive dialysis, the cancer albumin recovers its PSP-binding capacity. However, the possibility that some denaturation occurred during the alcohol treatment cannot be excluded. PSP binding to an abnormal globulin of a myelomatosis serum (H26) is probably a consequence of dehydration and precipitation of the myeloma protein. 

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