A Radioimmunoassay for Total Captopril in Human Serum or Plasma Samples

1984 ◽  
Vol 6 (1) ◽  
pp. 59-66 ◽  
Author(s):  
J. Tu ◽  
E. Liu ◽  
E. L. Nickoloff
Keyword(s):  
Human Serum ◽  
Plasma Samples

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.

LC–MS/MS measurement of 26 steroid hormones in human serum and plasma samples

2021 ◽  
Author(s):  
Yongjuan Jia ◽  
Xingli Liu ◽  
Li Xu ◽  
Jinbao Zhao ◽  
Junjun Ni ◽  
...  
Keyword(s):  
Human Serum ◽  
Steroid Hormones ◽  
Plasma Samples

Design and evaluation of standard lipid prediction models based on 1H-NMR spectroscopy of human serum/plasma samples

Metabolomics ◽  
2015 ◽  
Vol 11 (5) ◽  
pp. 1394-1404 ◽  
Author(s):  
Rubén Barrilero ◽  
Eduard Llobet ◽  
Roger Mallol ◽  
Jesús Brezmes ◽  
Lluis Masana ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Human Serum ◽  
1H Nmr ◽  
1H Nmr Spectroscopy ◽  
Prediction Models ◽  
Plasma Samples

scholarly journals Human Serum Albumin Cys34Oxidative Modifications following Infiltration in the Carotid Atherosclerotic Plaque

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Antonio Junior Lepedda ◽  
Angelo Zinellu ◽  
Gabriele Nieddu ◽  
Pierina De Muro ◽  
Ciriaco Carru ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carotid Endarterectomy ◽  
Atherosclerotic Plaque ◽  
Plasma Samples ◽  
Carotid Atherosclerotic Plaque ◽  
Sds Page ◽  
Oxidative Modifications ◽  
First Time

Objectives.To evaluate if the prooxidant environment present in atherosclerotic plaque may oxidatively modify filtered albumin.Methods.Fluorescein-5-maleimide labelled plasma samples and plaque extracts from 27 patients who had undergone carotid endarterectomy were analysed through nonreducing SDS-PAGE for albumin-Cys34oxidation. Furthermore, degree and pattern of S-thiolation in both circulating and plaque-filtered albumin were assayed.Results.Albumin filtered in the atherosclerotic plaque showed higher levels of Cys34oxidative modifications than the corresponding circulating form as well as different patterns of S-thiolation.Conclusions.Data indicate that the circulating albumin, once filtered in plaque, undergoes Cys34oxidative modifications and demonstrate for the first time that albumin is a homocysteine and cysteinylglycine vehicle inside the plaque environment.

A fully validated HPLC–UV method for determination of sulthiame in human serum/plasma samples

2020 ◽  
Author(s):  
Katarzyna Madej ◽  
Łukasz Paprotny ◽  
Dorota Wianowska ◽  
Joanna Kasprzyk ◽  
Małgorzata Herman ◽  
...  
Keyword(s):  
Human Serum ◽  
Plasma Samples

Effect of Severe Hypoxia on Blood-Cerebrospinal Fluid Barrier

1957 ◽  
Vol 190 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Lawrence B. Slobody ◽  
Dorothy C. Yang ◽  
Miriam Lending ◽  
Frank J. Borrelli ◽  
Marjorie Tyree
Keyword(s):  
Cerebrospinal Fluid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Concentration Ratio ◽  
Pressure Chamber ◽  
Severe Hypoxia ◽  
Plasma Samples ◽  
Intratracheal Administration ◽  
And Control

The effect of severe hypoxia on the blood-cerebrospinal fluid barrier of dogs was evaluated from the rate of passage of radioiodinated human serum albumin from plasma to cisternal fluid. Hypoxia was induced by intratracheal administration of varying mixtures of O2 and N2 or by use of a Smith-Jones pressure chamber. Radioiodinated albumin was injected intravenously and cisternal fluid and plasma samples were obtained at various intervals thereafter in experimental and control animals. Hypoxia maintained for 1 hour or longer resulted in a marked increase in the concentration ratio (cisternal fluid radioactivity)/(plasma radioactivity). The concentration ratio was frequently higher after 4 hours of hypoxia than after 24–48 hours in control animals. The slope of CSF albumin-I131 concentration as a function of time for the hypoxic animals was about five times that for the control animals. It is concluded that changes in rate of passage of albumin from plasma into cisternal fluid reflect alterations in the permeability of the blood-cerebrospinal fluid barrier to albumin.

Sign in / Sign up

Export Citation Format

Share Document