Structural Studies of Human IgG Myeloma Proteins of Different Antigenic Subgroups and Genetic Specificities

2015 ◽  
pp. 529-536
Author(s):  
H. H. Fudenberg ◽  
M. E. Koshland ◽  
B. Frangione ◽  
E. C. Franklin
Keyword(s):  
Structural Studies ◽  
Human Igg ◽  
Myeloma Proteins

scholarly journals STRUCTURAL STUDIES OF HUMAN IMMUNOGLOBULINS

1965 ◽  
Vol 122 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Blas Frangione ◽  
Edward C. Franklin
Keyword(s):  
Antigenic Specificity ◽  
Structural Studies ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Myeloma Proteins ◽  
Peptide Maps

1. Comparison of peptide maps of the Fc fragments of normal G immunoglobulins and 11 G myeloma proteins of the We (b) type showed them to be very similar except for differences associated with the Gm type. Some additional differences were noted, however, in the Fc fragments of three Vi (c) myeloma proteins. 2. Peptide maps of heavy chains from the same G myeloma proteins differed from each other and from normal heavy chains. In general, the myeloma chains contained a larger number of well defined spots; some of these were common to normal heavy chains while others were unique to each protein. Others, present in normal heavy chains, were lacking in the myeloma proteins. 3. Comparison of the heavy chains and Fc fragments from the same protein suggests that much of the variability of different myeloma proteins and, presumably, antibodies resides in the Fd fragment. 4. Further support for this is given by the finding that the antigenic specificity of 3 myeloma proteins also appeared to reside in the Fd fragments.

scholarly journals STRUCTURAL STUDIES OF HUMAN γG-MYELOMA PROTEINS OF DIFFERENT ANTIGENIC SUBGROUPS AND GENETIC SPECIFICITIES

1966 ◽  
Vol 124 (4) ◽  
pp. 715-732 ◽  
Author(s):  
B. Frangione ◽  
E. C. Franklin ◽  
H. H. Fudenberg ◽  
M. E. Koshland
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Heavy Chain ◽  
The Other ◽  
Structural Studies ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Methionine Sulfone ◽  
Peptide Maps ◽  
Heavy Chain Disease

1. Peptide maps of Fc fragments or heavy chains of 36 G myeloma proteins and two "heavy chain disease" proteins belonging to the four γ-chain subgroups revealed very striking similarities between them. However differences in a few peptides were noted. This was most pronounced for the Ge(γ2d) subgroup which lacked three peptides characteristic of the other three subgroups. While Fc fragments from different proteins belonging to the same subgroup appeared very similar, minor differences in addition to those based on currently recognized Gm factors were occasionally noted. 2. Fc fragments from Gm(a+) We(γ2b) proteins had a peptide previously shown to be characteristic of normal Gm(a+) γG-globulins. Fc fragments from Gm(a-) molecules belonging to the We(γ2b), Vi(γ2c), or Ne(γ2a) subgroups, whether Gm(b+), Gm(f+), or Gm(-), had the peptide previously identified in Gm(b+f+) normal γG-globulin. This "non-a" peptide was absent in peptide maps from Gm(-) molecules of the Ge(γ2d) subgroup which contained instead another peptide with the same electrophoretic mobility but migrating slightly further on chromatography. 3. Both the "a" and "non-a" peptides were pentapeptides having three amino acids in common, and differing in the other two. The "a" peptide contained one residue of lysine, aspartic acid, threonine, leucine, and glutamic acid. The "non-a" peptides prepared from Gm(b+), Gm(f+), and Gm(-) proteins were identical and contained one residue of lysine, threonine, and methionine sulfone, and two residues of glutamic acid. 4. Several possible mechanisms for the origin of these differences, and their possible role in serologic specificity are discussed.

Expression of F4, 8.12, 3I, and 16/6 Anti-DNA Idiotype-Related Antigens on Cationic Human IgG Myeloma Proteins

1994 ◽  
Vol 73 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Ralph C. Williams ◽  
Andrew D. Schriber ◽  
Christine C. Malone ◽  
Franco Silvestris ◽  
Noreen Hannigan ◽  
...  
Keyword(s):  
Human Igg ◽  
Myeloma Proteins

Crystals of Fragment Fab′: Preparation from Pepsin Digests of Human IgG Myeloma Proteins

Nature ◽  
1969 ◽  
Vol 223 (5208) ◽  
pp. 837-838 ◽  
Author(s):  
G. ROSSI ◽  
T. K. CHOI ◽  
A. NISONOFF
Keyword(s):  
Human Igg ◽  
Myeloma Proteins

scholarly journals GM AND INV FACTORS IN SUBCLASSES OF HUMAN IGG

1965 ◽  
Vol 122 (6) ◽  
pp. 1087-1102 ◽  
Author(s):  
William D. Terry ◽  
John L. Fahey ◽  
Arthur G. Steinberg
Keyword(s):  
Heavy Chain ◽  
Genetic Factors ◽  
Human Igg ◽  
Type K ◽  
Myeloma Proteins ◽  
Disease Protein ◽  
Polypeptide Chains ◽  
Heavy Chain Disease

Human G myeloma (7S γ2-myeloma) proteins were investigated for relationships between Gm and Inv genetic factors and the different antigenic types of heavy polypeptide chains (γ-chains) and light polypeptide chains. Myeloma proteins were isolated from the sera of 1 Chinese, 60 white and 28 Negro individuals. These 89 proteins were tested for eight Gm factors [Gm(a), Gm(x), Gm(b2), Gm(f), Gm(b1), Gm(b3), Gm(b4), and Gm(c)], and two Inv factors [Inv(l) and Inv(b)]. Results of the tests were correlated with the four γ-chain subclasses (γ2a, γ2b, γ2c and γ2d) and the two types of light polypeptide chains, κ-chains (type K or I) and λ-chains (type L or II) found in human IgG molecules. 1. Gm factors were limited to myeloma proteins with heavy polypeptide chains of the γ2b- and γ2c-subclasses. No Gm factors were detected on γ2a- and γ2d-myeloma proteins or on a "heavy-chain" disease protein of subclass γ2d. 2. γ2b-Proteins were positive for at least one Gm factor and were either Gm(a+), Gm(a + x+), or Gm(b2+ f+). 3. γ2c-Myeloma proteins, and one γ2c-"heavy-chain" disease protein, were positive for at least one Gm factor and contained various combinations of factors Gm(b1), (b2), (b4), and (c). Myeloma proteins from 3 Negroes were included in this group. 4. Inv factors (l) and (b) were limited to myeloma proteins with κ-light polypeptide chains. These Inv factors were not detected on proteins with λ-light polypeptide chains. 5. Most (70 per cent) of the γ2b- and γ2c-proteins with κ-chains were Inv(l+) or Inv(b+). None of the γ2a- or γ2d-proteins with κ-chains, however, contained these Inv factors.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Structural Studies on Mitotic Spindle Fibres

1978 ◽  
Vol 36 (3) ◽  
pp. 615-626
Author(s):  
J.R. Mcintosh
Keyword(s):  
Chemical Composition ◽  
Mitotic Spindle ◽  
Structural Studies ◽  
Mitotic Apparatus ◽  
Chemical Studies ◽  
Medical Interest ◽  
Spindle Fibres

The mitotic apparatus is a structure of obvious biological and medical interest, but it has proved to be a difficult cellular machine to understand. The chemical composition of the spindle is only slightly elucidated, largely because of the difficulties in preparing useful isolates of the structure. Chemical studies of the mitotic spindle have been reviewed elsewhere (Mcintosh, 1977), and will not be discussed further here. One would think that structural studies on the mitotic apparatus (MA) in situ would be straightforward, but even with this approach there is some disagreement in the results obtained with various methods and by different investigators. In this paper I will review briefly the approaches which have been used in structural studies of the MA, pointing out the strengths and problems of each approach. I will summarize the principal findings of the different methods, and identify what seem to be fruitful avenues for further work.

Sign in / Sign up

Export Citation Format

Share Document