Kinetics of five benzodiazepine hypnotics in healthy subjects

1983 ◽  
Vol 34 (1) ◽  
pp. 42-47 ◽  
Author(s):  
R Jochemsen ◽  
C J van Boxtel ◽  
J Hermans ◽  
D D Breimer
Keyword(s):  
Healthy Subjects ◽  
Kinetics Of

Kinetics of 111In-labelled platelets in healthy subjects

2009 ◽  
Vol 34 (5) ◽  
pp. 370-377 ◽  
Author(s):  
Kai Gjerløff Schmidt ◽  
Jens Waever Rasmussen ◽  
Anker Dahl Rasmussen
Keyword(s):  
Healthy Subjects ◽  
Kinetics Of

Absorption kinetics of oral and rectal flecainide in healthy subjects

1990 ◽  
Vol 38 (6) ◽  
pp. 595-598 ◽  
Author(s):  
L. Lie-A-Huen ◽  
J. H. Proost ◽  
J. H. Kingma ◽  
D. K. F. Meijer
Keyword(s):  
Healthy Subjects ◽  
Absorption Kinetics ◽  
Kinetics Of

Kinetics of G-CSF-induced granulocyte mobilization in healthy subjects: effects of route of administration and addition of dexamethasone

Transfusion ◽  
2002 ◽  
Vol 42 (5) ◽  
pp. 597-602 ◽  
Author(s):  
David F. Stroncek ◽  
Cynthia L. Matthews ◽  
Dean Follmann ◽  
Susan F. Leitman
Keyword(s):  
Healthy Subjects ◽  
Route Of Administration ◽  
Kinetics Of

Kinetics of intravenous and oral pentoxifylline in healthy subjects

1985 ◽  
Vol 37 (1) ◽  
pp. 25-28 ◽  
Author(s):  
Björn Beermann ◽  
Robert Ings ◽  
Jan Månsby ◽  
Joseph Chamberlain ◽  
Angela McDonald
Keyword(s):  
Healthy Subjects ◽  
Kinetics Of

Measurement of serum amyloid A1 (SAA1), a major isotype of acute phase SAA

2006 ◽  
Vol 44 (1) ◽  
Author(s):  
Yuanyuan Xu ◽  
Toshiyuki Yamada ◽  
Takahiko Satoh ◽  
Yasuaki Okuda
Keyword(s):  
Acute Phase ◽  
Healthy Subjects ◽  
Acute Phase Proteins ◽  
Serum Amyloid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Reactive Protein ◽  
Amyloid A ◽  
Amyloid Deposits ◽  
Clinical Conditions ◽  
Kinetics Of

AbstractSerum amyloid A (SAA), a plasma precursor of reactive amyloid deposits, is a multigene product. SAA1 and SAA2, with primary structures that are 93% identical (98 of 104 amino acids), behave as acute phase proteins, as demonstrated by their increasing levels in plasma. Heretofore, it has been understood that SAA1 predominates and functions as an isotype in plasma. However, accurate measurements differentiating the two isotypes have not been reported. In this study, using monoclonal antibodies specific for SAA1, we developed an enzyme-linked immunosorbent assay (ELISA) for SAA1. The levels and ratios of SAA1 in total SAA (TSAA) were investigated in healthy subjects and patients with rheumatoid arthritis (RA). The SAA1/TSAA ratio was 74±12% and 77±12% in healthy subjects and RA patients, respectively. In RA patients, the ratios were not influenced by SAA1 genotype, which has been proposed to affect plasma SAA values. The kinetics of SAA1 in inflamed patients undergoing hemodialysis was found to be parallel with total SAA and C-reactive protein. Finally, this study confirmed that SAA1 is a major isotype of acute phase SAA and may determine total SAA values. This specific assay could be used in the evaluation of SAA behavior in several clinical conditions.

scholarly journals The Slower Antibody Response in Myelofibrosis Patients after Two Doses of mRNA SARS-CoV-2 Vaccine Calls for a Third Dose

Biomedicines ◽  
2021 ◽  
Vol 9 (10) ◽  
pp. 1480
Author(s):  
Fabio Fiorino ◽  
Anna Sicuranza ◽  
Annalisa Ciabattini ◽  
Adele Santoni ◽  
Gabiria Pastore ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
Vaccine Dose ◽  
Antibody Responses ◽  
Inhibition Activity ◽  
Specific Antibodies ◽  
Slow Kinetics ◽  
Binding Inhibition ◽  
Specific Igg ◽  
The Impact ◽  
Kinetics Of

Immunization with mRNA SARS-CoV-2 vaccines has been highly recommended and prioritized in fragile subjects, including patients with myelofibrosis (MF). Available data on the vaccine immune response developed by MF patients and the impact of ruxolitinib treatment are still too fragmented to support an informed decision on a third dose for this category of subjects. Here, we show that 76% of MF patients develop spike-specific IgG after the second mRNA SARS-CoV-2 vaccine dose, but the response has a slower kinetics compared to healthy subjects, suggesting a reduced capability of their immune system to promptly react to vaccination. A reduced ACE2/RBD binding inhibition activity of spike-specific antibodies was also observed, especially in ruxolitinib-treated patients. Our results, showing slow kinetics of antibody responses in MF patients following vaccination with mRNA SARS-CoV-2 vaccines, support the need for a third vaccine dose.

Kinetics of plasma homocysteine in healthy subjects after peroral homocysteine loading

1993 ◽  
Vol 39 (7) ◽  
pp. 1390-1397 ◽  
Author(s):  
A B Guttormsen ◽  
A M Mansoor ◽  
T Fiskerstrand ◽  
P M Ueland ◽  
H Refsum
Keyword(s):  
Healthy Subjects ◽  
Volume Of Distribution ◽  
Plasma Homocysteine ◽  
Peroral Administration ◽  
Elimination Kinetics ◽  
Loading Test ◽  
Interindividual Variations ◽  
Health And Disease ◽  
Kinetics Of ◽  
Plasma Concentration Curve

Abstract The kinetics of plasma homocysteine were determined in 13 healthy subjects after peroral administration and in one person after intravenous injection. Various forms of homocysteine completely dissolved in an aqueous solution were rapidly absorbed after peroral administration, and the bioavailability was estimated to be 0.53. The volume of distribution was 0.66 L/kg. The area under the plasma concentration curve (AUC0-48 h) was proportional to the administered dose (33.5-134 mumol/kg body wt), and showed small interindividual variations. Plasma homocysteine showed first-order elimination kinetics for at least 6 h. The half-life (t1/2) was 223 +/- 45 min, and there was a significant correlation between t1/2 values determined on two different occasions in the same individual. The transient hyperhomocysteinemia was associated with an increase in plasma methionine, which probably reflects intracellular remethylation of homocysteine. Less than 2% of the administered homocysteine dose was recovered in the urine. These findings may form the basis for future studies on the regulation of plasma homocysteine in health and disease, and should motivate the evaluation of a homocysteine loading test as a diagnostic tool.

Redox status and protein binding of plasma aminothiols during the transient hyperhomocysteinemia that follows homocysteine administration

1993 ◽  
Vol 39 (6) ◽  
pp. 980-985 ◽  
Author(s):  
M A Mansoor ◽  
A B Guttormsen ◽  
T Fiskerstrand ◽  
H Refsum ◽  
P M Ueland ◽  
...  
Keyword(s):  
Protein Binding ◽  
Healthy Subjects ◽  
Normal Values ◽  
Oral Intake ◽  
Redox Status ◽  
Plasma Homocysteine ◽  
Moderate Increase ◽  
Similar Increase ◽  
Kinetics Of ◽  
Total Ratio

Abstract We administered reduced L-homocysteine perorally (67 mumol/kg of body wt) to 12 healthy subjects and injected the same dose into one person, and determined the kinetics of the alterations in reduced, oxidized, and protein-bound concentrations of homocysteine, cysteine, and cysteinylglycine. After oral intake, reduced homocysteine increased rapidly (tmax < or = 15 min), reaching concentrations [3.97 (SD 2.99) mumol/L] 20-fold above fasting values, and then declined towards the normal concentration within 2 h. There was a similar increase in reduced cysteine and a moderate increase in reduced cysteinylglycine. During this response, we observed a positive correlation between the reduced/total ratio for homocysteine and cysteine. When homocysteine was injected, the increase in reduced homocysteine preceded the increase in reduced cysteine by about 3 min. After oral loading, oxidized homocysteine showed a transient increase (tmax = 30 min) that lagged behind the increase of reduced homocysteine. Oxidized cysteine and cysteinylglycine were stable or decreased slightly. Protein-bound homocysteine increased the least rapidly after homocysteine administration (tmax = 1-2 h), and returned to normal values slowly. Changes in protein-bound homocysteine essentially mirrored a concurrent decrease in protein-bound cysteine, suggesting displacement of bound cysteine. These data show that plasma homocysteine has a pronounced, direct effect on the redox status and protein binding of other plasma thiol components. Such effects should be recognized when studying the mechanisms behind the atherogenic effect of increased plasma homocysteine.

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