Carrier Proteins of Folic Acid Activity in Human Serum

1971 ◽  
Vol 45 (2) ◽  
pp. 106-111 ◽  
Author(s):  
T. Markkanen ◽  
O. Peltola
Keyword(s):  
Folic Acid ◽  
Human Serum ◽  
Carrier Proteins

scholarly journals Development of a Sensitive Chemiluminescence Immunoassay for the Quantification of Folic Acid in Human Serum

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Xiang Chen ◽  
Qiyang Zhou ◽  
Ting Zhang ◽  
ChunXin Wang ◽  
Zheng Yu ◽  
...  
Keyword(s):  
Folic Acid ◽  
Horseradish Peroxidase ◽  
Human Serum ◽  
Magnetic Beads ◽  
Megaloblastic Anemia ◽  
Human Growth ◽  
Cross Reactivity ◽  
Alkaline Condition ◽  
Folate Binding Protein ◽  
Chemiluminescence Immunoassay

Folic acid (FA) is an important vitamin for human growth, especially for pregnant women. FA deficiency is associated with megaloblastic anemia, neural tube defects, cardiovascular diseases, irritability, diarrhea, and psychiatric disorders. Normally, FA molecules bind to folate-binding protein (FBP) in the serum as complex. Before quantify the FA concentration, a releasing procedure should be conducted. Alkaline condition and tris(2-carboxyethyl)phosphine (TCEP) are used to release binding FA to freeing state. In this work, a chemiluminescence immunoassay (CLIA) for human serum FA was established by competition model. Streptavidin (SA) was labeled to magnetic beads by an 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide/N-hydroxysuccinimide (EDAC/NHS) method. Activated biotin molecules were labeled to FBP molecules purified from milk. FA was labeled to horseradish peroxidase (HRP) by EDAC to activate the FA molecules. The pretreated samples or standards were added into the reaction tube with biotin-FBP and FA-horseradish peroxidase (HRP), FA in the sample compete with FA-HRP for binding to biotin-FBP, the signal is inversely proportional to the FA concentration. The method established shows good thermostability and performance. The limitation of detection (LOD) is 0.44 ng/mL. The intra-assay coefficient of variation (CV) is 3.6%–7.1%, the interassay CV is 4.2%–7.5%, and the recovery rate is 92.1%–103.5%. Cross reactivity (CR) was remarkably low with aminopterin, folinic acid, and methotrexate. The method shows good correlation with the FA CLIA product from Beckman Coulter; the equation is y = 0.9618x−0.1434 while the R2 value is 0.9224. The established method is sensitive, rapid, and accurate which can fully satisfy for the clinical requirement.

scholarly journals Dihydro-sphingosine 1-phosphate interacts with carrier proteins in a manner distinct from that of sphingosine 1-phosphate

2018 ◽  
Vol 38 (5) ◽  
Author(s):  
Yuko Mishima ◽  
Makoto Kurano ◽  
Tamaki Kobayashi ◽  
Masako Nishikawa ◽  
Ryunosuke Ohkawa ◽  
...  
Keyword(s):  
Human Serum ◽  
Clinical Significance ◽  
Knockout Mice ◽  
Plasma Samples ◽  
Carrier Proteins ◽  
Serum Samples ◽  
Apolipoprotein M ◽  
Physiological Properties ◽  
Specific Manner ◽  
Sphingosine 1 Phosphate

Dihydro-sphingosine 1-phosphate (DH-S1P) is an analog of sphingosine 1-phosphate (S1P), which is a potent lysophospholipid mediator. DH-S1P has been proposed to exert physiological properties similar to S1P. Although S1P is known to be carried on HDL via apolipoprotein M (apoM), the association between DH-S1P and HDL/apoM has not been fully elucidated. Therefore, in the present study, we aimed to elucidate this association and to compare it with that of S1P and HDL/apoM. First, we investigated the distributions of S1P and DH-S1P among lipoproteins and lipoprotein-depleted fractions in human serum and plasma samples and observed that both S1P and DH-S1P were detected on HDL; furthermore, elevated amounts of DH-S1P in serum samples were distributed to the lipoprotein-depleted fraction to a greater degree than to the HDL fraction. Concordantly, a preference for HDL over albumin was only observed for S1P, and not for DH-S1P, when the molecules were secreted from platelets. Regarding the association with HDL, although both S1P and DH-S1P prefer to bind to HDL, HDL preferentially accepts S1P over DH-S1P. For the association with apoM, S1P was not detected on HDL obtained from apoM knockout mice, while DH-S1P was detected. Moreover, apoM retarded the degradation of S1P, but not of DH-S1P. These results suggest that S1P binds to HDL via apoM, while DH-S1P binds to HDL in a non-specific manner. Thus, DH-S1P is not a mere analog of S1P and might possess unique clinical significance.

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 Folic acid receptor-targeted human serum albumin nanoparticle formulation of cabazitaxel for tumor therapy

2018 ◽  
Vol Volume 14 ◽  
pp. 135-148 ◽  
Author(s):  
Yating Sun ◽  
Yarong Zhao ◽  
Shanshan Teng ◽  
Fei Hao ◽  
Huan Zhang ◽  
...  
Keyword(s):  
Folic Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Tumor Therapy ◽  
Acid Receptor ◽  
Nanoparticle Formulation ◽  
Folic Acid Receptor

scholarly journals Adsorptive stripping voltammetric assay of folic acid in human serum

1988 ◽  
Vol 6 (6-8) ◽  
pp. 743-747 ◽  
Author(s):  
J.M.Fernandez Alvarez ◽  
A.Costa Garcia ◽  
A.J.Miranda Ordieres ◽  
Paulino Tuñón Blanco
Keyword(s):  
Folic Acid ◽  
Human Serum ◽  
Voltammetric Assay

Transferrin, the Third Carrier Protein of Folic Acid Activity in Human Serum

1972 ◽  
Vol 48 (4) ◽  
pp. 213-217 ◽  
Author(s):  
T. Markkanen ◽  
S. Virtanen ◽  
P. Himanen ◽  
R.-L Pajula
Keyword(s):  
Folic Acid ◽  
Human Serum ◽  
Carrier Protein ◽  
The Third

Detection of folic acid protein in human serum using reduced graphene oxide electrodes modified by folic-acid

2016 ◽  
Vol 75 ◽  
pp. 389-395 ◽  
Author(s):  
Lijie He ◽  
Qian Wang ◽  
Daniel Mandler ◽  
Musen Li ◽  
Rabah Boukherroub ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Folic Acid ◽  
Human Serum ◽  
Reduced Graphene Oxide ◽  
Oxide Electrodes ◽  
Acid Protein ◽  
Reduced Graphene
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