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.

scholarly journals Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment

1968 ◽  
Vol 106 (1) ◽  
pp. 15-21 ◽  
Author(s):  
B. Frangione ◽  
C. Milstein ◽  
Edward C. Franklin
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
The Other ◽  
Light Chains ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Other Hand ◽  
Terminal Loop ◽  
Heavy Chain Disease

The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present. The sequences appear to be identical in the Fc fragments of two types of chain studied (γ1 and γ3), and very similar to corresponding sequences of the Fc fragment in rabbit. These results suggest that the C-terminal half of the heavy chains is covalently folded (in a similar fashion to the light chains) with a C-terminal loop and an N-terminal loop. The similarity is emphasized by comparison of the sequence and location of the disulphide-bridged peptides of the C-terminal loop of heavy and light chains. The N-terminal loop, on the other hand, appears to be very different in Fc fragments and light chains. The C-terminal loop is the only one present in the F′c fragment.

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 The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes

1967 ◽  
Vol 105 (3) ◽  
pp. 1019-1028 ◽  
Author(s):  
J. W. Prahl
Keyword(s):  
Gene Duplication ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Disease Protein ◽  
Heavy Chain Disease

The sequences of the C-terminal octadecapeptides obtained by cyanogen bromide cleavage of the γ-chains of myeloma proteins of the four subclasses, and a urinary heavy-chain-disease protein, have been determined. Although the sequences were markedly homologous, unique replacements were identified that distinguished between the γ2b, γ2c and γ2d subclasses. The data are in accord with the postulated existence of four genetic loci or cistrons, these having arisen by the process of gene duplication.

scholarly journals SIX BALB/c IgA MYELOMA PROTEINS THAT BIND ß-(1 → 6)-D-GALACTAN

1973 ◽  
Vol 138 (5) ◽  
pp. 1095-1106 ◽  
Author(s):  
Stuart Rudikoff ◽  
Elizabeth B. Mushinski ◽  
Michael Potter ◽  
C. P. J. Glaudemans ◽  
Michael E. Jolley
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Heavy Chain ◽  
Antigenic Determinant ◽  
Amino Acid Sequences ◽  
The Other ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Highly Sensitive

Six IgA myeloma proteins of BALB/c origin which bind antigens containing ß-(1 → 6)-D-galactan side chains have been isolated by affinity chromatography on galactoside-BSA-Sepharose columns. Partial amino acid sequences of of the light chains to residue Cys23 and the heavy chains to reside 30 were determined on the automated sequencer. No differences were found among the six VK sequences. Among some 50 partial VK sequences that have thus far been determined these six chains are the only ones thus far identified in this subgroup; at least 25 VK subgroups in the mouse have been identified so far. The heavy chain partial sequences were also very closely related but two differences were found. One protein differed from the other five by having isoleucine instead of leucine at position 5, a second protein differed from the others by having an unidentified amino acid at position 19. Using the highly sensitive inhibition of hemagglutination method it was found that each of the proteins possessed a unique inidividual antigenic determinant.

scholarly journals Amino acid sequence of the N-terminal sixty-nine residues of heavy chain derived from a homogeneous rabbit antibody

1972 ◽  
Vol 130 (2) ◽  
pp. 539-546 ◽  
Author(s):  
Jean-Claude Jaton ◽  
D. G. Braun
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Heavy Chain ◽  
Sequence Variation ◽  
Sequence Variability ◽  
Rabbit Antibody ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Variable Section ◽  
Chain Sequence

The sequence of the N-terminal 69 residues of heavy chain from a homogeneous rabbit antibody to type III pneumococcal polysaccharide was determined. The sequence is similar to that found in heavy chains of normal pooled rabbit immunoglobulins of the same allotype Aa1. Two regions of the homogeneous heavy chain (residues 35–46 and 62–69) are very similar to corresponding regions of heavy chains from rabbit Aa2 immunoglobulin, as well as from mouse, guinea-pig and human immunoglobulins. In contrast, residues 47–62 appear to be variable. Comparison in this section with another homogeneous anti-pneumococcal antibody (Strosberg et al., 1972) of related specificity and of the same allotype indicates sequence variation in at least three positions. An antibody to group C streptococcal carbohydrate of allotype Aa2 (Fleischman, 1971) differs by five amino acids in the same region of the heavy chain. Sequence variability between these three antibodies does not occur in homologous positions within this variable section. Allotype-related sequences could not be identified in section 34–65.

Displacement of Valine From Intact Sea-Urchin Eggs by Exogenous Amino Acids

1968 ◽  
Vol 3 (4) ◽  
pp. 515-527
Author(s):  
J. PIATIGORSKY ◽  
A. TYLER
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Sea Urchin ◽  
Sea Water ◽  
The Other ◽  
Metabolic Product ◽  
Primary Factor ◽  
Lytechinus Pictus ◽  
Sea Urchin Eggs ◽  
Neutral Amino Acids

Unfertilized and fertilized eggs of the sea urchin Lytechinus pictus were preloaded with [14C]valine and exposed to individual solutions of each of the twenty ‘coded’ [12C]amino acids in artificial sea water. After 1 h incubation the amount of radioactivity in the medium was determined. The radioactivity was effectively displaced by most of the other neutral [12C]amino acids that are known to compete with valine for uptake. A chromatographic test with fertilized eggs showed the displaced radioactivity to be [14C]valine and not some metabolic product. Addition of acidic, basic or some neutral amino acids that are known to be poor inhibitors of valine uptake did not cause significant quantities of label to appear in the medium. For the unfertilized eggs, the concentration of acid-soluble label remained many hundreds of times greater in the egg fluid than in the sea water. Tests indicated that efflux of [14C]valine and subsequent competition for re-entry is a primary factor responsible for the displacement phenomenon. That this may not be the sole factor is suggested by the fact that some amino acids that are known to be powerful inhibitors of valine uptake were found to be only weak displacers of [14C]valine. Neither [14C]arginine nor [14C]glutamic acid were displaced in significant amounts from preloaded unfertilized or fertilized eggs by any of the tested [12C]amino acids. Attempts were made to utilize the displacement of [12C]valine to elevate the incorporation of [14C]valine and of other labelled amino acids into protein by intact eggs. Unfertilized and fertilized eggs were pretreated with related [12C]amino acids and then exposed to [14C]valine or a mixture of [14C]amino acids. The results varied in the different tests, ranging from no significant increase to 2-fold.

A 59-Year-Old Woman With Immunotactoid Glomerulopathy, Heavy-Chain Disease, and Non-Hodgkin Lymphoma

2004 ◽  
Vol 128 (6) ◽  
pp. 689-692
Author(s):  
Erica Jacobson ◽  
Gregory Sharp ◽  
Jeffrey Rimmer ◽  
Bruce MacPherson
Keyword(s):  
Hodgkin Lymphoma ◽  
Heavy Chain ◽  
Average Diameter ◽  
World Health ◽  
Heavy Chains ◽  
Non Hodgkin Lymphoma ◽  
Immunotactoid Glomerulopathy ◽  
History Of ◽  
Health Organization ◽  
Heavy Chain Disease

Abstract Immunotactoid glomerulopathy is one of several renal disorders characterized by the extracellular deposition of nonamyloid fibrillary deposits. There is considerable debate as to whether immunotactoid glomerulopathy should be distinguished from fibrillary glomerulonephritis, a closely related entity. Currently, the distinction is based on fibril size and arrangement. We report the case of a 59-year-old woman in whom a diagnosis of immunotactoid glomerulopathy was made after a 2-year history of proteinuria. Electron microscopy of her renal biopsy showed randomly arranged microtubular subepithelial and mesangial deposits, which measured 34 nm in average diameter. She was later discovered to have circulating immunoglobulin G heavy chains without associated light chains (γ-heavy-chain disease) and, subsequently, non-Hodgkin lymphoma, follicular lymphoma, grade I (World Health Organization classification). Approximately 100 cases of γ-heavy-chain disease have been reported in the literature since it was originally described by Franklin in 1964. However, while there are 10 reports in the literature of heavy-chain disease with fibrillary deposits in the kidney, none fit the criteria for immunotactoid glomerulopathy.

scholarly journals Arrangement of the disulphide bridges in human low-Mr kininogen

1987 ◽  
Vol 247 (1) ◽  
pp. 15-21 ◽  
Author(s):  
J Kellermann ◽  
C Thelen ◽  
F Lottspeich ◽  
A Henschen ◽  
R Vogel ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Light Chain ◽  
The Other ◽  
Critical Importance

The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.

Nitrogen requirements of the fungal endophytes of Arundina chinensis

1971 ◽  
Vol 49 (3) ◽  
pp. 407-410 ◽  
Author(s):  
R. C. Stephen ◽  
K. K. Fung
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Yeast Extract ◽  
Organic Nitrogen ◽  
Fungal Endophytes ◽  
Nitrogen Sources ◽  
The Other ◽  
Atmospheric Nitrogen

The nitrogen requirements of two Rhizoctonia fungus endophytes of the orchid Arundina chinensis are reported. Both isolates were capable of using ammonium and organic nitrogen but not nitrate or atmospheric nitrogen. Glutamic acid and urea were the best of the nitrogen sources tested followed by arginine, then asparagine. Proline and methionine were not used. The addition of a mixture of vitamins to the amino acids increased growth of one of the isolates but not the other. Yeast extract supported greatest growth.

Sign in / Sign up

Export Citation Format

Share Document