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

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

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.

scholarly journals Pharmaceutical immunoglobulin G impairs anti-carcinoma activity of oxaliplatin in colon cancer cells

2021 ◽  
Author(s):  
Yuru Shang ◽  
Xianbin Zhang ◽  
Lili Lu ◽  
Ke Jiang ◽  
Mathias Krohn ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Viability ◽  
Cancer Patients ◽  
Cell Lines ◽  
Cancer Cell ◽  
Immunoglobulin G ◽  
Cancer Cell Lines ◽  
Human Igg ◽  
Western Blots ◽  
Igg Receptors

Abstract Background Recent evidence proves that intravenous human immunoglobulin G (IgG) can impair cancer cell viability. However, no study evaluated whether IgG application benefits cancer patients receiving chemotherapeutics. Methods Influence of pharmaceutical-grade human IgG on the viability of a series of patient-derived colon cancer cell lines with and without chemotherapeutic intervention was determined. Cell death was analysed flow cytometrically. In addition, the influence of oxaliplatin and IgG on the ERK1/2-signalling pathway was evaluated by western blots. Results We evaluated the effects of pharmaceutical IgG, such as PRIVIGEN® IgG and Tonglu® IgG, in combination with chemotherapeutics. We did not observe any significant effects of IgG on tumour cell viability directly; however, human IgG significantly impaired the anti-tumoral effects of oxaliplatin. Primary cancer cell lines express IgG receptors and accumulate human IgG intracellularly. Moreover, while oxaliplatin induced the activation of ERK1/2, the pharmaceutical IgG inhibited ERK1/2 activity. Conclusions The present study demonstrates that pharmaceutical IgG, such as PRIVIGEN® IgG and Tonglu® IgG, can impair the anti-carcinoma activity of oxaliplatin. These data strongly suggest that therapeutic IgG as co-medication might have harmful side effects in cancer patients. The clinical significance of these preclinical observations absolutely advises further preclinical, as well as epidemiological and clinical research.

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