scholarly journals The Stability of Parathyroid Hormone in Blood and Serum Samples at 4°C and at Room Temperature

1995 ◽  
Vol 32 (2) ◽  
pp. 216-217 ◽  
Author(s):  
D Russell ◽  
R Henley
Keyword(s):  
Parathyroid Hormone ◽  
Room Temperature ◽  
Serum Samples ◽  
The Stability

scholarly journals Stability of Parathyroid Hormone-Related Protein and Parathyroid Hormone at Room Temperature

1994 ◽  
Vol 31 (5) ◽  
pp. 497-500 ◽  
Author(s):  
G E Levin ◽  
J A Nisbet
Keyword(s):  
Parathyroid Hormone ◽  
Protease Inhibitor ◽  
Room Temperature ◽  
Related Protein ◽  
Blood Samples ◽  
Parathyroid Hormone Related Protein ◽  
Edta Plasma ◽  
The Stability ◽  
Serum Pth ◽  
Zero Time

The stability of plasma parathyroid hormone-related protein (PTHrP) as measured by the Nichols Institute assay at room temperature was assessed over a period of 72 h in blood samples collected in protease inhibitor tubes and EDTA tubes at 0, 6, 24, 48 and 72 h from 10 patients with hypercalcaemia of malignancy. Mean plasma PTHrP concentrations in blood samples collected in protease inhibitor tubes remained stable for up to 48 h but had decreased by 10% at 72 h. The mean EDTA plasma PTHrP at zero time was 67% of the protease inhibitor tube value and this had fallen to 39% at 72 h. The stability of parathyroid hormone (PTH) in separated blood samples was also assessed by collection into heparin and plain tubes as well as EDTA and protease inhibitor tubes. Serum PTH concentrations progressively declined throughout the 72 h study period although the zero time values were significantly higher than corresponding plasma PTH concentrations. Plasma PTH concentrations appeared to be stable when blood was collected in heparin, EDTA and protease inhibitor tubes during the 72 h period, except in one subject with markedly elevated plasma amylase activity.

Stability of immunologic activity of human prostatic acid phosphatase in serum.

1982 ◽  
Vol 28 (5) ◽  
pp. 1163-1166 ◽  
Author(s):  
I W Chen ◽  
M I Sperling ◽  
H R Maxon ◽  
L A Kaplan
Keyword(s):  
Acid Phosphatase ◽  
Room Temperature ◽  
Chelating Agent ◽  
Prostatic Acid Phosphatase ◽  
Storage Conditions ◽  
Enzymic Activity ◽  
Serum Samples ◽  
Long Term Storage ◽  
The Stability ◽  
Immunologic Activity

Abstract The stability of the immunologic activity of human serum prostatic acid phosphatase (iPAP;EC 3.1.3.2) under various storage conditions was evaluated. Although more stable than the enzymic activity of serum PAP, serum iPAP was inactivated rapidly at room temperature at neutral and especially at alkaline pH. Purified iPAP in a phosphate buffer (pH 7.5) was stable for at least three days at room temperature but showed instability similar to that of serum iPAP when added to heat-treated serum (30 min at 56 degrees C, pH 8.3). Addition of a protease inhibitor, a sulfhydryl agent, or a chelating agent failed to preserve iPAP. Acidification of serum with an acetate buffer (5 mol/L, pH 5.0), 20 microliters/mL of serum, protected but could not restore serum iPAP activity. When stored at 24 degrees C, serum iPAP was most stable at pH 6.5. Acidification had little effect on PAP values by radioimmunoassay, iPAP values from acidified and unacidified serum samples being essentially the same. We recommend that blood samples drawn for PAP immunoassays be kept at 4 degrees C and that serum samples be separated and acidified as soon as practical. For long-term storage, acidified serum samples should be kept in small aliquots at -20 or -70 degrees C.

scholarly journals Analytical Validation of a New Immunoenzymatic Method for the Measurement of Feline Parathyroid Hormone in Cats with Chronic Kidney Disease

Animals ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 3100
Author(s):  
Jari Zambarbieri ◽  
Pierangelo Moretti ◽  
Alessia Giordano ◽  
Paola Scarpa
Keyword(s):  
Chronic Kidney Disease ◽  
Parathyroid Hormone ◽  
Kidney Disease ◽  
Diagnostic Procedures ◽  
Renal Diseases ◽  
Good Precision ◽  
Analytical Validation ◽  
Serum Samples ◽  
Immunoenzymatic Method ◽  
The Stability

The determination of parathyroid hormone (PTH) in cats could be of clinical utility in many metabolic disorders, such as renal diseases, hypercalcemia, or nutritional imbalances. However, the available methods for the measurement of feline PTH are limited, not widely available, and need radioimmunoassays. The aim of this study was to perform the analytical validation of a new immunoenzymatic method for the measurement of feline PTH. Thirty-eight cats affected with chronic kidney disease (CKD) were included. PTH was measured using a two-site immunoenzymatic method validated in humans and dogs (ST AIA-PACK® Intact PTH, Tosoh Bioscience, Tessenderlo, Belgium). The analytical validation provided the evaluation of precision (intra-assay and inter-assay), accuracy (linearity under dilution (LUD) and spike recovery test (SRT)), and the storage stability of serum samples at 20 °C, 4 °C, and −20 °C. The method showed good precision (intra-assay CVs (coefficient of variations) 3.19–9.61%; inter-assay CVs 9.26–15.28%). In both the intra- and inter-assays, the highest imprecision was found with the low concentration pool (9.61% and 15.28%) and accuracy (LUD and SRT r2 = 0.99, p < 0.001), while the stability was optimal up until 7 days at −20 °C (−7.7%). The method was successfully validated in cats, allowing its future use in diagnostic procedures.

The Stability of Creatine Kinase Isoenzymes Studied with Two-Site Monoclonal Antibody Assays

1985 ◽  
Vol 22 (3) ◽  
pp. 310-315 ◽  
Author(s):  
A P Jackson ◽  
R J Thompson
Keyword(s):  
Monoclonal Antibody ◽  
Creatine Kinase ◽  
Room Temperature ◽  
Storage Conditions ◽  
Normal Serum ◽  
Serum Samples ◽  
Subunit Dissociation ◽  
Creatine Kinase Isoenzymes ◽  
Antibody Assays ◽  
The Stability

The stability of human creatine kinase isoenzymes was investigated under different storage conditions using specific two-site monoclonal antibody assays. In Tris-HCl buffer pH 7·5 or barbitone buffer pH 8·1 containing 5 g/L bovine serum albumin, the isoenzymes appeared to be stable for up to 3 weeks at 4°C but suffered a partial subunit dissociation and random reassociation after freeze–thawing; this dissociation was more pronounced as a result of freezing at −20°C rather than at −70°C. In contrast, creatine kinase isoenzymes stored in serum were stable at both 4°C and following freeze-thawing. High levels of heart type creatine kinase in serum showed only minor subunit hybridisation even after 12 h at room temperature. We conclude that in practical clinical situations, subunit hybridisation in serum samples is negligible. We recommend however, that isoenzyme standards for use in either two-site assays or radioimmunoassays should be stored frozen in normal serum from which endogenous creatine kinase isoenzymes have been previously removed.

scholarly journals Stability of parathyroid hormone ex vivo in haemodialysis patients

2003 ◽  
Vol 40 (2) ◽  
pp. 191-193 ◽  
Author(s):  
T. K. Teal ◽  
M. Reed ◽  
P. E. Stevens ◽  
E. J. Lamb
Keyword(s):  
Parathyroid Hormone ◽  
Room Temperature ◽  
Ex Vivo ◽  
Renal Dialysis ◽  
Blood Collection ◽  
Dialysis Patients ◽  
Edta Plasma ◽  
The Stability ◽  
End Stage ◽  
Blood Collection Tubes

Background: The stability of parathyroid hormone (PTH) in blood ex vivo is a significant practical problem for laboratories and clinicians. Several studies have suggested that PTH is more stable in blood collected into a potassium edetate (EDTA) preservative. Methods: To confirm that this was applicable to renal dialysis patients using our assay (Nichols chemiluminescence), we examined PTH stability in 13 patients with end-stage renal failure using three different blood collection tubes. Results: PTH remained stable in EDTA plasma for up to 48 h at room temperature. PTH was significantly reduced in serum collected into plain tubes after 2 h, and after 4 h in serum collected into serum separator tubes, at room temperature. Conclusion: In the assessment of renal osteodystrophy, the use of EDTA plasma can confer significant benefit, especially in busy laboratories where rapid frozen separation of blood may be hard to achieve.

Methods for the Concentration of Bovine Ac-Globulin (Factor V)

1961 ◽  
Vol 06 (03) ◽  
pp. 435-444 ◽  
Author(s):  
Ricardo H. Landaburu ◽  
Walter H. Seegers
Keyword(s):  
Room Temperature ◽  
Barium Carbonate ◽  
Deae Cellulose ◽  
Reducing Agents ◽  
Factor V ◽  
Isoelectric Precipitation ◽  
Stabilizing Agent ◽  
Bovine Plasma ◽  
The Stability

SummaryAn attempt was made to obtain Ac-globulin from bovine plasma. The concentrates contain mostly protein, and phosphorus is also present. The stability characteristics vary from one preparation to another, but in general there was no loss before 1 month in a deep freeze or before 1 week in an icebox, or before 5 hours at room temperature. Reducing agents destroy the activity rapidly. S-acetylmercaptosuccinic anhydride is an effective stabilizing agent. Greatest stability was at pH 6.0.In the purification bovine plasma is adsorbed with barium carbonate and diluted 6-fold with water. Protein is removed at pH 6.0 and the Ac-globulin is precipitated at pH 5.0. Rivanol and alcohol fractionation is followed by chromatography on Amberlite IRC-50 or DEAE-cellulose. The final product is obtained by isoelectric precipitation.

Tyrosine-Selective Bioconjugation with Iminoxyl Radicals

2020 ◽  
Author(s):  
Katsuya Maruyama ◽  
Takashi Ishiyama ◽  
Yohei Seki ◽  
Kounosuke Oisaki ◽  
Motomu Kanai
Keyword(s):  
Reaction Time ◽  
Steric Hindrance ◽  
Room Temperature ◽  
Water Soluble ◽  
Light Irradiation ◽  
Sodium Ascorbate ◽  
Iminoxyl Radical ◽  
Short Reaction Time ◽  
Modified Peptides ◽  
The Stability

A novel Tyr-selective protein bioconjugation using the water-soluble persistent iminoxyl radical is described. The conjugation proceeded with high Tyr-selectivity and short reaction time under biocompatible conditions (room temperature in buffered media under air). The stability of the conjugates was tunable depending on the steric hindrance of iminoxyl. The presence of sodium ascorbate and/or light irradiation promoted traceless deconjugation, restoring the native Tyr structure. The method is applied to the synthesis of a protein-dye conjugate and further derivatization to azobenzene-modified peptides.

Circular dichroism and infrared study of β-turn formation in repeat peptides of elastin

1987 ◽  
Vol 52 (5) ◽  
pp. 1356-1361
Author(s):  
S. Abdel Rahman ◽  
M. Elsafty ◽  
A. Hattaba
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Ir Spectra ◽  
Chain Length ◽  
Room Temperature ◽  
Infrared Study ◽  
Feature Characteristic ◽  
C 50 ◽  
The Stability ◽  
Circular Dichroïsm

The conformation of elastin-like peptides Boc-Ala-Pro-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM were examined in solution using circular dichroism at 30 °C, 50 °C, and 70 °C and in solid state by IR at room temperature. The studies show that the β-turn is a significant conformational feature for peptides under investigation in solution at 30 °C and 50 °C, but at 70 °C the tetra, hexa, and decapeptides show the CD feature characteristic of the β-structure while the dodecapeptide spectra show the presence of β-turn which indicates the stability of the β-turn at this chain length. The IR spectra show that in the solid state at room temperature all investigated peptides assume essentially a β-turn except the tetrapeptide which present evidence of antiparallel β-structure. The β-turn contribution in the IR spectra increases with the increase of the chain length of the peptide.

Cholesterol in Serum and Lipoprotein Fractions

1956 ◽  
Vol 2 (3) ◽  
pp. 145-159 ◽  
Author(s):  
Joseph T Anderson ◽  
Ancel Keys
Keyword(s):  
Human Serum ◽  
Total Cholesterol ◽  
Filter Paper ◽  
Room Temperature ◽  
Paper Electrophoresis ◽  
Cholesterol Content ◽  
Intraindividual Variability ◽  
Detailed Data ◽  
The Stability ◽  
Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

Pressure dependent ultrasonic properties of hcp hafnium metal

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Ramanshu P. Singh ◽  
Shakti Yadav ◽  
Giridhar Mishra ◽  
Devraj Singh
Keyword(s):  
Elastic Constants ◽  
Pressure Range ◽  
Room Temperature ◽  
Ultrasonic Attenuation ◽  
Coupling Constants ◽  
Ultrasonic Properties ◽  
Acoustic Coupling ◽  
Third Order Elastic Constants ◽  
The Stability ◽  
The Given

Abstract The elastic and ultrasonic properties have been evaluated at room temperature between the pressure 0.6 and 10.4 GPa for hexagonal closed packed (hcp) hafnium (Hf) metal. The Lennard-Jones potential model has been used to compute the second and third order elastic constants for Hf. The elastic constants have been utilized to calculate the mechanical constants such as Young’s modulus, bulk modulus, shear modulus, Poisson’s ratio, and Zener anisotropy factor for finding the stability and durability of hcp hafnium metal within the chosen pressure range. The second order elastic constants were also used to compute the ultrasonic velocities along unique axis at different angles for the given pressure range. Further thermophysical properties such as specific heat per unit volume and energy density have been estimated at different pressures. Additionally, ultrasonic Grüneisen parameters and acoustic coupling constants have been found out at room temperature. Finally, the ultrasonic attenuation due to phonon–phonon interaction and thermoelastic mechanisms has been investigated for the chosen hafnium metal. The obtained results have been discussed in correlation with available findings for similar types of hcp metals.

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