scholarly journals Method development of immunoglobulin G purification from micro-volumes of human serum for untargeted and targeted proteomics-based antibody repertoire studies

2019 ◽  
Vol 27 (2) ◽  
pp. 475-482
Author(s):  
Yu-Ting Chang ◽  
Ming-Chu Chang ◽  
Yun-Jung Tsai ◽  
Christine Ferng ◽  
Hsi-Chang Shih ◽  
...  
Keyword(s):  
Human Serum ◽  
Immunoglobulin G ◽  
Method Development ◽  
Antibody Repertoire ◽  
Targeted Proteomics

LC-MSMS Method Development for Steroids Panel Analysis in Human Serum.

2010 ◽  
pp. P3-41-P3-41
Author(s):  
Hua-fen Liu ◽  
John McFarlane ◽  
Renee Huang ◽  
Adam Latawiec ◽  
Lisa Sapp
Keyword(s):  
Human Serum ◽  
Method Development ◽  
Panel Analysis

Binding of enzyme--IgG complexes in human serum to Protein-A Sepharose CL-4B.

1980 ◽  
Vol 26 (2) ◽  
pp. 297-300
Author(s):  
K Bauer ◽  
P M Bayer ◽  
E Deutsch ◽  
F Gabl
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Human Serum ◽  
Immunoglobulin G ◽  
Protein A ◽  
The Other ◽  
Routine Method ◽  
Simple Method ◽  
Human Serum Protein ◽  
Enzyme Complexes

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.

Autoantibodies to thyroxin and triiodothyronine in the immunoglobulin G fraction of serum.

1988 ◽  
Vol 34 (12) ◽  
pp. 2561-2562 ◽  
Author(s):  
L Li Calzi ◽  
S Benvenga ◽  
S Battiato ◽  
F Santini ◽  
F Trimarchi
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Hormones ◽  
Human Serum ◽  
Immunoglobulin G ◽  
Subacute Thyroiditis ◽  
Total Serum ◽  
Graves Disease ◽  
Carrier Proteins ◽  
Weak Binding ◽  
Idiopathic Myxedema

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.

scholarly journals Prolactin-immunoglobulin G complexes from human serum act as costimulatory ligands causing proliferation of malignant B lymphocytes.

1995 ◽  
Vol 92 (8) ◽  
pp. 3278-3282 ◽  
Author(s):  
A. M. Walker ◽  
D. W. Montgomery ◽  
S. Saraiya ◽  
T. W. Ho ◽  
H. S. Garewal ◽  
...  
Keyword(s):  
Human Serum ◽  
B Lymphocytes ◽  
Immunoglobulin G

A new approach to the depletion of albumin and immunoglobulin G from human serum

2015 ◽  
Vol 51 (3) ◽  
pp. 367-373 ◽  
Author(s):  
E. A. Bormotova ◽  
B. L. Mil’man ◽  
T. V. Gupalova
Keyword(s):  
Human Serum ◽  
Immunoglobulin G ◽  
New Approach

A V region-connected autoreactive subfraction of normal human serum immunoglobulin G

1992 ◽  
Vol 22 (7) ◽  
pp. 1701-1706 ◽  
Author(s):  
Gilles Dietrich ◽  
Srinivas-Venkatesh Kaveri ◽  
Michel D. Kazatchkine
Keyword(s):  
Human Serum ◽  
Immunoglobulin G ◽  
Normal Human Serum ◽  
Serum Immunoglobulin ◽  
Normal Human ◽  
V Region

Method Development and Validation for Ultra-High-Pressure LC/MS/MS Determination of Hop Prenylflavonoids in Human Serum

2012 ◽  
Vol 95 (6) ◽  
pp. 1744-1749 ◽  
Author(s):  
Yang Yuan ◽  
Xi Qiu ◽  
Dejan Nikolic ◽  
Jeffrey H Dahl ◽  
Richard B van Breemen
Keyword(s):  
High Pressure ◽  
Human Serum ◽  
Method Development ◽  
Hot Flashes ◽  
Cancer Chemoprevention ◽  
Gradient Elution ◽  
Negative Ion ◽  
Selected Reaction Monitoring ◽  
Ultra High Pressure

Abstract Hops (Humulus lupulus L.) are used in the brewing of beer, and hop extracts containing prenylated compounds, such as xanthohumol (XN) and 8-prenylnaringenin (8-PN), are under investigation as dietary supplements for cancer chemoprevention and the management of hot flashes in menopausal women. To facilitate clinical studies of hop safety and efficacy, a selective, sensitive, and fast ultra-high-pressure LC (UHPLC) tandem MS method was developed and validated for the simultaneous determination of the hop prenylflavonoids XN, isoxanthohumol (IX), 6-prenylnaringenin (6-PN), and 8-PN in human serum. The analytical method requires 300 μL of human serum, which is processed using liquid–liquid extraction. UHPLC separation was carried out in 2.5 min with gradient elution using an RP C18 column containing 1.6 μm particle size packing material. Prenylflavonoids were measured using negative ion electrospray MS with collision-induced dissociation and selected reaction monitoring. The method was validated and showed good accuracy and precision with an LOQ of 0.50 ng/mL for XN (1.4 nM) and 1.0 ng/mL for 6-PN, 8-PN (2.94 nM), and IX (2.82 nM) in serum.

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