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.

Stability of total cholesterol, high-density-lipoprotein cholesterol, and triglycerides in frozen sera.

1986 ◽  
Vol 32 (6) ◽  
pp. 995-999 ◽  
Author(s):  
Y M Stokes ◽  
C E Salmond ◽  
L M Carpenter ◽  
T J Welby
Keyword(s):  
High Density Lipoprotein ◽  
Human Serum ◽  
Sample Size ◽  
Total Cholesterol ◽  
High Density Lipoprotein Cholesterol ◽  
Density Lipoprotein ◽  
High Density ◽  
Lipoprotein Cholesterol ◽  
The Stability

Abstract When human serum must be stored for extended periods before analysis, conditions must be such that samples give results comparable with those for "fresh" (unstored) samples. In a balanced experiment with statistically pre-determined sample size, we assessed, at three-weekly intervals for 18 weeks, the stability of total cholesterol, high-density-lipoprotein cholesterol, and triglycerides in human serum stored at -15 degrees C. No significant changes were observed.

An evaluation of the stability of factor VIII inhibitors in plasma and plasma dried on filter paper discs stored at room temperature

Haemophilia ◽  
2003 ◽  
Vol 9 (1) ◽  
pp. 57-59 ◽  
Author(s):  
R. Winikoff ◽  
A. Boulanger ◽  
J. St Louis ◽  
S. Lacroix ◽  
G.-É. Rivard
Keyword(s):  
Factor Viii ◽  
Filter Paper ◽  
Room Temperature ◽  
The Stability

SEM Observations on the Germination of Euonymous Americanus

1985 ◽  
Vol 43 ◽  
pp. 508-509
Author(s):  
D.R. Hill ◽  
J.R. McCurry ◽  
L.P. Elliott ◽  
G. Howard
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Light Microscopy ◽  
Filter Paper ◽  
Room Temperature ◽  
Food Source ◽  
Environmental Chamber ◽  
Dormant Stage ◽  
Scanning Electron

Germination of Euonymous americanus in the laboratory has previously been unsuccessful. Ability to germinate Euonymous americanus. commonly known as the american strawberry bush, is important in that it represents a valuable food source for the white-tailed deer. Utilizing the knowledge that its seeds spend a period of time in the rumin fluid of deer during their dormant stage, we were successful in initiating germination. After a three month drying period, the seeds were placed in 25 ml of buffered rumin fluid, pH 8 at 40°C for 48 hrs anaerobically. They were then allowed to dry at room temperature for 24 hrs, placed on moistened filter paper and enclosed within an environmental chamber. Approximately four weeks later germination was detected and verified by scanning electron microscopy; light microscopy provided inadequate resolution. An important point to note in this procedure is that scarification, which was thought to be vital for germination, proved to be unnecessary for successful germination to occur. It is believed that germination was propagated by the secretion of enzymes or prescence of acids produced by microorganisms found in the rumin fluid since sterilized rumin failed to bring about germination.

Human Blood Serum Rich in Factor V

1970 ◽  
Vol 24 (03/04) ◽  
pp. 334-337 ◽  
Author(s):  
R Honorato
Keyword(s):  
Blood Serum ◽  
Human Serum ◽  
Human Blood ◽  
Human Blood Serum ◽  
Factor V ◽  
The Stability

Summary1. A technique to obtain human serum rich in factor V is described.2. Calcium increases the stability of factor V in the serum.

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.

scholarly journals 68Ga, 44Sc and 177Lu-labeled AAZTA5-PSMA-617: synthesis, radiolabeling, stability and cell binding compared to DOTA-PSMA-617 analogues

2020 ◽  
Vol 5 (1) ◽  
Author(s):  
Jean-Philippe Sinnes ◽  
Ulrike Bauder-Wüst ◽  
Martin Schäfer ◽  
Euy Sung Moon ◽  
Klaus Kopka ◽  
...  
Keyword(s):  
Human Serum ◽  
Room Temperature ◽  
Solid Phase ◽  
Negative Influence ◽  
Binding Motif ◽  
Lncap Cells ◽  
Cell Binding ◽  
Binding Characteristics

Abstract Background The AAZTA chelator and in particular its bifunctional derivative AAZTA5 was recently investigated to demonstrate unique capabilities to complex diagnostic and therapeutic trivalent radiometals under mild conditions. This study presents a comparison of 68Ga, 44Sc and 177Lu-labeled AAZTA5-PSMA-617 with DOTA-PSMA-617 analogues. We evaluated the radiolabeling characteristics, in vitro stability of the radiolabeled compounds and evaluated their binding affinity and internalization behavior on LNCaP tumor cells in direct comparison to the radiolabeled DOTA-conjugated PSMA-617 analogs. Results AAZTA5 was synthesized in a five-step synthesis and coupled to the PSMA-617 backbone on solid phase. Radiochemical evaluation of AAZTA5-PSMA-617 with 68Ga, 44Sc and 177Lu achieved quantitative radiolabeling of > 99% after less than 5 min at room temperature. Stabilities against human serum, PBS buffer and EDTA and DTPA solutions were analyzed. While there was a small degradation of the 68Ga complex over 2 h in human serum, PBS and EDTA/DTPA, the 44Sc and 177Lu complexes were stable at 2 h and remained stable over 8 h and 1 day. For all three compounds, i.e. [natGa]Ga-AAZTA5-PSMA-617, [natSc]Sc-AAZTA5-PSMA-617 and [natLu]Lu-AAZTA5-PSMA-617, in vitro studies on PSMA-positive LNCaP cells were performed in direct comparison to radiolabeled DOTA-PSMA-617 yielding the corresponding inhibition constants (Ki). Ki values were in the range of 8–31 nM values which correspond with those of [natGa]Ga-DOTA-PSMA-617, [natSc]Sc-DOTA-PSMA-617 and [natLu]Lu-DOTA-PSMA-617, i.e. 5–7 nM, respectively. Internalization studies demonstrated cellular membrane to internalization ratios for the radiolabeled 68Ga, 44Sc and 177Lu-AAZTA5-PSMA-617 tracers (13–20%IA/106 cells) in the same range as the ones of the three radiolabeled DOTA-PSMA-617 tracers (17–20%IA/106 cells) in the same assay. Conclusions The AAZTA5-PSMA-617 structure proved fast and quantitative radiolabeling with all three radiometal complexes at room temperature, excellent stability with 44Sc, very high stability with 177Lu and medium stability with 68Ga in human serum, PBS and EDTA/DTPA solutions. All three AAZTA5-PSMA-617 tracers showed binding affinities and internalization ratios in LNCaP cells comparable with that of radiolabeled DOTA-PSMA-617 analogues. Therefore, the exchange of the chelator DOTA with AAZTA5 within the PSMA-617 binding motif has no negative influence on in vitro LNCaP cell binding characteristics. In combination with the faster and milder radiolabeling features, AAZTA5-PSMA-617 thus demonstrates promising potential for in vivo application for theranostics of prostate cancer.

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