scholarly journals 174: LONGITUDINAL CHANGES OF NEURO-SPECIFIC SERUM PROTEINS IN COVID-19 PATIENTS

2021 ◽  
Vol 50 (1) ◽  
pp. 71-71
Author(s):  
Mariana Restrepo ◽  
Tony Okeke ◽  
Kumal Siddiq ◽  
Pranav Tadikonda ◽  
Krzysztof Laudanski
Keyword(s):  
Serum Proteins ◽  
Longitudinal Changes ◽  
Specific Serum

scholarly journals The Protein Corona of PEGylated PGMA-Based Nanoparticles is Preferentially Enriched with Specific Serum Proteins of Varied Biological Function

Langmuir ◽  
2017 ◽  
Vol 33 (45) ◽  
pp. 12926-12933 ◽  
Author(s):  
Priya S. R. Naidu ◽  
Marck Norret ◽  
Nicole M. Smith ◽  
Sarah A. Dunlop ◽  
Nicolas L. Taylor ◽  
...  
Keyword(s):  
Biological Function ◽  
Serum Proteins ◽  
Protein Corona ◽  
Specific Serum

Optimizing Nephelometric Measurement of Specific Serum Proteins: Evaluation of Three Diluents

1974 ◽  
Vol 20 (12) ◽  
pp. 1548-1552 ◽  
Author(s):  
Lawrence M Killingsworth ◽  
Gregory J Buffone ◽  
Meena B Sonawane ◽  
Glennie C Lunsford
Keyword(s):  
Steady State ◽  
Continuous Flow ◽  
Reaction Rate ◽  
Serum Proteins ◽  
Physiological Saline ◽  
Rate Analysis ◽  
Specific Serum ◽  
State Approximation ◽  
Α2 Macroglobulin ◽  
Steady State Approximation

Abstract Three diluents were studied, to determine which is the best for the automated immunochemical measurement of specific serum proteins. Nine serum proteins (orosomucoid, α1-antitrypsin, α2-macroglobulin, haptoglobin, transferrin, C3, IgG, IgA, and IgM) were measured in physiological saline (9 g NaCI/liter), tris(hydroxymethyl)aminomethane buffer (0.01 mol/liter; pH 7.4), and physiological saline containing polyethylene glycol ("PEG 6000," 40 g/liter). Criteria were: reaction rate, analysis rate, carryover between samples, steady-state approximation, precision, and correlation with other methods. Saline containing polyethylene giycol is the best of the three diluents for use in continuous-flow nephelometric analysis of serum proteins.

The Transport of Thyroid Hormones

1983 ◽  
Vol 65 (4) ◽  
pp. 337-342 ◽  
Author(s):  
R. Hoffenberg ◽  
D. B. Ramsden
Keyword(s):  
Thyroid Hormones ◽  
Binding Proteins ◽  
Serum Proteins ◽  
High Capacity ◽  
Free Fraction ◽  
Total Serum ◽  
Free T4 ◽  
Specific Serum ◽  
Target Organs ◽  
Serum T4

1. Hormones have to be transported from their sites of synthesis to their target organs. For lipophilic hormones, such as steroids and thyroid hormones, transport is accomplished by binding to specific serum proteins, in the case of thyroxine (T4) and tri-iodothyronine (T3) to thyroxine-binding globulin (TBG) and prealbumin (PA). Normally about 70% of circulating T4 and 75–80% of T3 is bound to TBG, about 20% of T4 and 10% of T3 to PA and 10–15% of each to albumin, which has a low affinity but high capacity for both hormones [1, 2]. Apart from facilitating transport, binding to serum protein prevents excessive loss of hormone into the urine by glomerular filtration or flooding into cells, and may provide a readily available reservoir in times of need. The union between binding proteins and their ligands is reversible, so that a small proportion of hormone is non-protein-bound or ‘free’, in equilibrium with that which is protein-bound. For T4 this free fraction is normally 0.02-0.04% of the total serum T4 concentration, for T3 about 0.3% [3, 4]. 2. The major binding proteins of T4 and T3 will briefly be described and the nature of free T4 and T3 considered.

151 PROTEOMICS ANALYSIS OF PREGNANCY-SPECIFIC SERUM PROTEINS IN BOVINE

2006 ◽  
Vol 18 (2) ◽  
pp. 183 ◽  
Author(s):  
D. I. Jin ◽  
H. R. Lee ◽  
H. R. Kim ◽  
H. J. Lee ◽  
J. T. Yoon ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Early Pregnancy ◽  
Serum Proteins ◽  
Optical Resolution ◽  
Variable Region ◽  
Serum Samples ◽  
Proteomics Analysis ◽  
Specific Serum ◽  
Specific Proteins ◽  
Immunoglobulin Gamma

To identify early pregnancy-specific serum proteins in bovine, we performed proteomics analysis using blood serum samples of pregnant and non-pregnant Holstein dairy cattle Days 21 and 35 after AI. A total of eight pregnant and eight non-pregnant cattle were used for collection of the blood samples. The global proteomics approach was exploited by the use of 2-D gel electrophoresis and mass spectrometry to sort out pregnancy-specific proteins. Serum proteins within isoelectric point ranges of 4.0 to 7.0, 6.0 to 9.0, and 5.5 to 6.7 were analyzed separately by 2-D electrophoresis with three replications of each sample. The stained gels were scanned and calibrated at an optical resolution of 63.5 �m/pixel using a GS-710 imaging densitometer (Bio-Rad Laboratories, Philadelphia, PA, USA). A total of approximately 1200 spots were detected in 2-D gels stained with Coomassie-blue. In the comparison of serum samples from pregnant and non-pregnant cattle, nine pregnancy-specific spots were detected unanimously in Day 21 and Day 35 serum samples. Pregnancy-specific proteins were identified as transferrin, albumin, IgG2a heavy chain constant region, and immunoglobulin gamma heavy chain variable region by means of MALDI-TOF-MS (PerSeptive Biosystems, Framingham, MA, USA). Even though the identified spots were abundant serum proteins, their molecular weights and pI values were different from those of the main serum proteins. Most proteins identified in this analysis appeared to be related with pregnancy-specific subunits or fragments of transferrin, albumin, and IgG. One of the pregnancy-specific proteins, transferrin, is known to be related to iron transport during pregnancy. Western blot analysis using polyclonal anti-transferrin antibody revealed specific transferrin expression in the serum samples from the pregnant cattle but no detectable expression in the serum samples from the non-pregnant cattle. Our results revealed composite profiles of key proteins involved in early pregnancy and suggest the potential use of identified proteins to detect early pregnancy in bovine.

scholarly journals Specific Protein Determinations Using Immunoelectrophoresis

1973 ◽  
Vol 10 (1-6) ◽  
pp. 4-13 ◽  
Author(s):  
Margaret J. Driscoll
Keyword(s):  
Sex Hormones ◽  
Diagnostic Tool ◽  
Serum Proteins ◽  
Specific Protein ◽  
Control Population ◽  
Reference Ranges ◽  
Specific Serum ◽  
Hospital Patients ◽  
Healthy Persons

The Laurell ‘rocket’ technique of immunoelectrophoresis has been used to quantitate seven specific serum proteins in a control population of SO healthy persons and in 100 hospital patients. Reference ranges have been established for each protein from data obtained from the control population. For many of the proteins variations due to age and/or sex were observed. Sex hormones, probably oestrogens, were also observed to cause variations in some of the protein concentrations. Data obtained from the hospital patients indicated that further work should prove profitable and could enable specific protein determinations to be useful, both as a diagnostic tool and in following the course of a disease.

Induction of female-specific serum proteins in the sand lamprey,Lampetra reissneri, by exogenous estradiol-17β

1987 ◽  
Vol 34 (2) ◽  
Author(s):  
Shoichi Fukayama ◽  
Akihiko Hara ◽  
Takahiro Matsubara ◽  
Hiroya Takahashi
Keyword(s):  
Serum Proteins ◽  
Specific Serum ◽  
Female Specific ◽  
Estradiol 17Β

Automated Quantitative Immunochemical Analysis of Human Immunoglobulins

1972 ◽  
Vol 18 (11) ◽  
pp. 1364-1367 ◽  
Author(s):  
Harold Markowitz ◽  
A R Tschida
Keyword(s):  
Continuous Flow ◽  
Serum Proteins ◽  
Immunochemical Analysis ◽  
Cerebrospinal Fluid Proteins ◽  
Automated Method ◽  
Specific Serum ◽  
Human Immunoglobulins ◽  
Precise Estimation ◽  
Manual Methods

Abstract A commercial automated continuous-flow procedure for estimating specific serum proteins has been evaluated for use in determination of IgG, IgA, IgM (both 19S and 7S), α1-antitrypsin, and cerebrospinal fluid proteins. Results of the automated procedure correlate well with manual methods, but are much more precise. Estimation of 7S IgM by the automated method is more accurate than estimation by radial immunodiffusion, because concentrations of 7S IgM are not spuriously elevated.

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