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

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.

1967 ◽  
Vol 105 (3) ◽  
pp. 1019-1028 ◽  
Author(s):  
J. W. Prahl

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.


Blood ◽  
1975 ◽  
Vol 46 (1) ◽  
pp. 1-9 ◽  
Author(s):  
RM Lyons ◽  
H Chaplin ◽  
TW Tillack ◽  
PW Majerus

Abstract A patient, CAL, with gamma heavy chain disease is presented who has had a complete remission lasting over 2 yr with combination chemotherapy consisting of pulsatile cyclophosphamide and prednisone. The patient exhibited many features of an atuoimmune process including a vasculitis, low serum complement levels, a positive antiglobulin (Coombs) test, Raynaud's phenomenon, and keratoconjunctivitis sicca. The CAL paraprotein was found to have several previously undescribed characteristics. It reacted with antisera to Fd, Fab, and Fab', suggesting that most of the Fd portion of the molecule was intace. CAL protein consists of two polypeptide chains of molecular weight 49,000 covalently linked to form a dimer of 95,000 molecular weight. The covalent linkage suggests that the hinge region of this gamma heavy chain is intact.


1984 ◽  
Vol 30 (12) ◽  
pp. 2021-2025 ◽  
Author(s):  
P Blangarin ◽  
P Deviller ◽  
K Kindbeiter ◽  
J J Madjar

Abstract We used two-dimensional polyacrylamide gel electrophoresis and immunoblotting techniques to study serum proteins from a patient with a monoclonal gammopathy. Two-dimensional electrophoresis was optimized for serum proteins with two main goals: (a) to allow the resolution of many serum proteins in both directions, with penetration of the maximum number of proteins in the first dimension; and (b) to obtain the best reproducibility from one experiment to another, within the limits of the current technique. These analyses, combined with immunoblotting, permitted us to characterize a gamma heavy chain disease protein of 34 000-Da molecular mass. Moreover, two-dimensional mapping of the patient's serum proteins allowed demonstration of the microheterogeneity of this monoclonal component.


1976 ◽  
Vol 13 (3) ◽  
pp. 245-249 ◽  
Author(s):  
Yoko Nabeshima ◽  
Tokuji Ikenaka ◽  
Terukatsu Arima

1990 ◽  
Vol 27 (8) ◽  
pp. 771-776 ◽  
Author(s):  
C. Mihaesco ◽  
P. Ferrara ◽  
J.C. Guillemot ◽  
N. Congy ◽  
M.C. Gendron ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document