Purification of polyclonal Immunoglobulin G from human serum using peptide‐based adsorbents

AIChE Journal ◽  
2021 ◽  
Author(s):  
Wenning Chu ◽  
Sobhana A. Sripada ◽  
Hannah R. Reese ◽  
Dipendra Bhandari ◽  
Augustus Adams ◽  
...  
2011 ◽  
Vol 46 (1) ◽  
pp. 101-107 ◽  
Author(s):  
Rattana Wongchuphan ◽  
Beng Ti Tey ◽  
Wen Siang Tan ◽  
Senthil Kumar Subramanian ◽  
Farah Saleena Taip ◽  
...  

2019 ◽  
Vol 27 (2) ◽  
pp. 475-482
Author(s):  
Yu-Ting Chang ◽  
Ming-Chu Chang ◽  
Yun-Jung Tsai ◽  
Christine Ferng ◽  
Hsi-Chang Shih ◽  
...  

1994 ◽  
Vol 67 (800) ◽  
pp. 770-774 ◽  
Author(s):  
A Jiménez-Heffernan ◽  
J L Villanueva ◽  
A Moral ◽  
A Rebollo ◽  
F M González ◽  
...  

2020 ◽  
Author(s):  
Anri Sawada ◽  
Masayoshi Okumi ◽  
Shigeru Horita ◽  
Tomomi Tamura ◽  
Sekiko Taneda ◽  
...  

Abstract The authors have withdrawn this preprint due to author disagreement.


1980 ◽  
Vol 26 (2) ◽  
pp. 297-300
Author(s):  
K Bauer ◽  
P M Bayer ◽  
E Deutsch ◽  
F Gabl

Abstract We describe a simple method for detecting enzyme--immunoglobulin G (IgG) complexes in human serum. Protein-A Sepharose CL-4B binds IgG and therefore also the enzyme--IgG complexes, which can then be separated easily from the serum by centrifugation. We demonstrate this separation in two patients, one with a complex of IgG and creatine kinase (EC 2.7.3.2) BB isoenzyme, the other with an IgG--alkaline phosphatase (EC 3.1.3.1) complex. Both patients had unexplainably high activities of the respective enzymes in their serum. The method we propose should be a useful, simple, routine method of detection in cases where IgG--enzyme complexes are suspected.


1988 ◽  
Vol 34 (12) ◽  
pp. 2561-2562 ◽  
Author(s):  
L Li Calzi ◽  
S Benvenga ◽  
S Battiato ◽  
F Santini ◽  
F Trimarchi

Abstract Thyroid hormone antibodies (THAbs)--i.e., antibodies to thyroxin (T4) and triiodothyronine (T3)--are detected rarely in human serum, where they are searched for, possibly because of a quantitatively minimal interaction between thyroid hormones (the haptens) and serum IgGs (the antibodies). The weak binding could result from these facts: (a) there are already six physiological carrier proteins for thyroid hormones; (b) THAbs usually account for a very small fraction of the total serum IgGs; (c) THAbs may have--as reported in the literature--a relatively low affinity. To ascertain whether THAbs could pass undetected in serum, we measured antibodies to T3 and T4 in both the serum and the corresponding IgG fraction of six normal persons and 45 patients with various thyroid diseases (Graves' disease, idiopathic myxedema, Hashimoto's thyroiditis, subacute thyroiditis, tumors), using radioimmunoprecipitation. The prevalence of antibodies to T4 was 0/51 in both the sera and the IgG fractions; the prevalence of antibodies to T3 was 1/51 in both materials. Because all of the sera that tested THAb negative were confirmed to be so in the THAb assay of the IgG fraction, we conclude that the prevalence of serum THAbs is not underestimated and that autoimmunization against thyroid hormones is really a rare phenomenon.


2020 ◽  
Vol 70 (7) ◽  
pp. 463-469
Author(s):  
Hirofumi Watanabe ◽  
Yoichi Takeuchi ◽  
Shinji Taniuchi ◽  
Hiroshi Sato ◽  
Yasuhiro Nakamura ◽  
...  

Placenta ◽  
2019 ◽  
Vol 83 ◽  
pp. e86-e87
Author(s):  
Carlos Mario Rodríguez Colorado ◽  
Manuela Velasquez Berrío ◽  
Diana Carolina Rúa Molina ◽  
Angela María Álvarez Gomez ◽  
Angela Patricia Cadavid Jaramillo

Sign in / Sign up

Export Citation Format

Share Document