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At least 307 records · Page 17Linked to original sources
PubMed1983

Seasonal effect on steroids in blood plasma and seminal plasma of boars.

Unconjugated testosterone (T), 5a-androst-16-en-3-one (delta-16), dihydrotestosterone (DHT), unconjugated (u Oe) and conjugated oestrogens (c Oe) were determined weekly in the peripheral blood plasma and seminal plasma of 8 boars for a period of 15 months. Four of the boars were kept under natural daylength fluctuations (8-17 h), and 4 boars on a light programme which shifted these fluctuations by half a year. In peripheral plasma of all boars the highest concentrations were found for c Oe (17 ng/ml) followed by delta-16 (7.3), T (2.2) DHT (0.75) and u Oe (0.24). In seminal plasma of all boars (with an average volume of 172 ml) the highest concentrations were again found for c Oe (5.9 ng/ml) followed by delta-16 (1.1), u Oe (0.73), T (0.28) and DHT (0.1). This shows that u Oe reach higher concentrations in seminal plasma than in blood plasma. In boars under the influence of natural daylight steroids fluctuated with season. Maximum concentrations were present from October till December. Minimum concentrations were about 1/10 of the maximum concentrations. All steroids measured in blood and semen were similarly affected and all were highly correlated. In boars on an artificial light programme the off-season depression during the summer was completely restored. This indicates that daylight fluctuations are the main reason for seasonal changes of testicular function in the domestic boar.

Androgens↗
PubMed2004

Application of liquid-phase microextraction and gas chromatography-mass spectrometry for the determination of polychlorinated biphenyls in blood plasma.

This study investigated the feasibility of applying liquid-phase microextraction combined with gas chromatography-mass spectrometry (GC-MS) to determine polychlorinated biphenyls (PCBs) in blood plasma. An efficient and simple extraction technique has been developed for the enrichment of PCBs from human blood plasma samples using single-step liquid-phase microextraction (LPME) in conjunction with a hollow fibre membrane (HFM). An eight PCB congener mixture was spiked into 2.5 ml of blood plasma, and the solution was then adjusted to pH 10.5 with a salinity of 20% (w/v) prior to making the total volume to 5 ml with ultrapure water. The porous HFM, filled with 3 microl of organic solvent, was then immersed into the solution, which was continuously agitated at 700 rpm for 30 min. Extract (1 microl) containing the pre-concentrated analytes was then injected into a GC-MS without further pre-treatment. Using an optimised extraction procedure, a large enrichment factor of the analytes, i.e. up to 241-fold was achieved in 30 min. The procedure resulted in a relative standard deviation of < 11% (n = 6), and a linear calibration range from 2.5 to 150 microg/l (r > 0.999), and detection limits between 0.07 and 0.94 microg/l, respectively. To demonstrate the feasibility of the procedure, PCB concentrations were determined in actual blood samples collected from the local population in Singapore using the optimised LPME technique.

Gas Chromatography-Mass Spectrometry↗
PubMed1997

One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centred radicals.

Exposure of human blood plasma to peroxynitrite in the presence of 3,5-dibromo-4-nitrosobenzenesulphonic acid (DBNBS) resulted in the trapping of a strongly immobilized nitroxide radical adduct. The adduct was due to protein-centred radicals derived not only from serum albumin but also from other major plasma proteins (fibrinogen, IgG, alpha1-antitrypsin and transferrin). Urate significantly protected plasma from the peroxynitrite-induced DBNBS-plasma protein adduct, whereas ascorbate and glutathione were protective at concentrations exceeding those usually found in plasma. Alkylation of plasma -SH groups did not affect the intensity of DBNBS-plasma protein adduct, whereas bicarbonate increased its formation, thus showing a pro-oxidant effect. The DBNBS-plasma protein adduct provided little structural information, but subsequent non-specific-protease treatment resulted in the detection of an isotropic three-line spectrum, indicating the trapping of radicals centred on a tertiary carbon. The nitrogen hyperfine coupling constant of this adduct and its superhyperfine structure were similar to those of DBNBS-tryptophan peptides with the alpha-amino group of tryptophan linked in the amide bond, consistent with a radical adduct formed at C-3 of the indole ring of tryptophan-containing peptides. DBNBS was unable to trap radicals derived from peroxynitrite-treated tyrosine or tyrosine-containing peptides. Methionine treated with peroxynitrite resulted in the trapping of at least two DBNBS-methionine adducts with hyperfine structures different from that of protease-treated DBNBS-plasma proteins. These results demonstrate that peroxynitrite induced in blood plasma the formation of protein radicals centred on tryptophan residues and underline the relevance of the one-electron oxidation pathway of peroxynitrite decomposition in biological fluids.

Ascorbic Acid↗
PubMed1993

Retinals and retinols induced by estrogen in the blood plasma of Xenopus laevis.

Injection of estrogen into male Xenopus laevis induced the appearance of retinals (retinal and 3-dehydroretinal) and a considerable increase in the amount of retinols (retinol and 3-dehydroretinol) in the blood plasma. These retinoids were mainly in the all-trans form. Without estrogen injection, retinols were normally found in the blood plasma of both males and females, but only trace amounts of retinals were detected and these were restricted to the plasma of females. The proteins in the blood plasma of estrogen-injected males were separated into two fractions. One fraction included vitellogenin, the precursor of egg yolk proteins, and the other contained some plasma proteins other than vitellogenin. Retinals were detected in the former and retinols in the latter. It is suggested that retinals are bound to vitellogenin and are taken up into oocytes in the process of vitellogenesis.

Animals↗
PubMed2006

Sex steroids level in blood plasma and ovarian follicles of the chimeric chicken.

The study was performed to determine the hormonal status of mature germline chimeras obtained by blastodermal cell transfer from chicken embryos of a donor breed [Green-legged Partridgelike breed (GP) x Araucana (AR)] to those of a recipient breed [White Leghorn (WL)] being at the same stage of embryonic development. The egg-laying chimeras and WL hens (control) of the same age were used in the experiment. At first, blood samples were taken from each bird at 0.5, 5, 12.5 and 18.5 h following oviposition. Subsequently, the chimeras and the WL hens were decapitated 1-2 h after ovulation. A stroma and the following follicles were isolated from the ovary: white normal (1-4, 4-6 and 6-8 mm), white atretic and yellow preovulatory follicles (F4-F1). Sex hormones, progesterone (P4), testosterone (T) and oestradiol (E2) in blood plasma and ovarian follicles were determined radioimmunologically. The activity of the 3beta-hydroxysteroid dehydrogenase (3beta-HSD) in the granulosa and theca layers of the follicles was analysed histochemically. In chimeric chickens, a higher level of T in blood plasma during the ovulatory cycle was noticed. However, in the stroma, white prehierarchical and medium-size preovulatory ovarian follicles the level of T was significantly lower. With respect to E2, its elevated levels were found both in blood and in the ovarian follicles. There were no significant differences in P4 concentrations in blood plasma while in ovarian follicles a higher level was observed only in white 6-8 mm follicles. 3beta-HSD activity in granulosa and theca layers of the ovarian follicles in chimeras was not different from that in the WL hens. In conclusion, the results obtained indicate that germline chimeras exhibit significant alterations in sex hormone levels in the ovary and blood plasma, which in turn may affect their reproductive abilities.

Animals↗
PubMedDate not supplied

[Activity of amine oxidases from blood plasma and thrombocytes in sensitization and allergy].

Activities of amine oxidase from blood plasma and of monoamine oxidase from thrombocytes were studied in persons sensitized to yeast fungus and in patients with allergic diseases. Activity of the blood plasma amine oxidase tended to increase in sensitization and to decrease in patients with allergic dermatoses. In this group of patients activity of the thrombocyte monoamine oxidase was higher as compared with that of healthy persons.

Amine Oxidase (Copper-Containing)↗
PubMed1985

The effect of beta carotene supplementation on the beta carotene and vitamin A levels of blood plasma and some fertility indices of dairy cows.

Seasonal variations in beta carotene intake and low levels of beta carotene and vitamin A in blood plasma were found in cows fed ration based mainly on maize silage. The supplementation of daily winter rations with 300 mg Rovimix-beta carotene per cow, beginning 14 days before parturition and 60 days after calving increased slighty the beta carotene and vitamin A concentrations of blood plasma and improved some fertility indices: the number of inseminations per cow was reduced and the percentage of conception rate was significantly higher. It may be assumed that beta carotene content in feeds and it's utilization rate generally reflected in beta carotene blood plasma level and in the improvement of fertility.

Animal Feed↗
PubMed1989

Multivariate calibration for assays in clinical chemistry using attenuated total reflection infrared spectra of human blood plasma.

A spectral analysis of human blood plasma was undertaken by use of a Fourier-transform infrared spectrometer with a circular attenuated total reflection cell. The concentrations of total protein, glucose, triglycerides, total cholesterol, urea, and uric acid were measured by chemical or enzymatic methods. For these constituents the partial least-squares (PLS) algorithm was used for a multivariate calibration including the infrared fingerprint region of the plasma spectra. Best results were achieved for total protein with an average prediction error (PRESS based on cross validation) of 2.1 g/L; other PRESS results were for glucose 22 mg/dL, triglycerides 33 mg/dL, cholesterol 31 mg/dL, urea 4.4 mg/dL, and uric acid 1.6 mg/dL.

Algorithms↗
PubMed2006

Blood plasma contact activation on silicon, titanium and aluminium.

In the present work, blood plasma protein deposition to spontaneously air oxidized silicon, titanium and aluminium was re-investigated in vitro. Immunological- and null ellipsometry methods were used to detect and quantitate adsorbed proteins, RIA methods to study the retention of preadsorbed 125I-HSA upon exposure to buffer or blood plasma, and kallikrein-specific colorimetric substrate S-2302 to follow the surface generation of kallikrein. The results show that the contact activation of coagulation and complement systems are connected on Si and Ti, but not on Al, via coagulation factor XII. Preadsorbed 125I-HSA was most readily displaced on silicon, followed by titanium and aluminium. The surfaces displayed different antibody binding patterns after short and long-time exposures to plasma. Titanium and silicon bound anti-HMWK after 1 min in plasma, but aluminium did not. When the plasma incubation time was prolonged up to 2h the anti-HMWK binding disappeared totally on titanium and decreased on silicon. During the same time period, anti-C3c binding increased to the three types of surfaces. Also, the anti-C3c binding onto Si and Ti, but not Al, disappeared after incubation in Factor XII deficient plasma or when a specific coagulation factor XII (Factor XII) inhibitor, corn trypsin inhibitor (CTI) was added to normal plasma. The surface contacted plasmas cleaved the kallikrein-specific reagent S-2302 both after single surface contact, and after reincubation of surfaces in fresh plasma. The results show that C3b and Factor XIIa and their degradation products were retained at the surfaces.

Adsorption↗
PubMed1975

Corticosteroids in nocturnal blood plasma of cows in the field related to stage of lactation and plasma acetoacetate.

Two materials of nocturnal blood plasma samples, each representing more than 100 cows unselected with respect to health condition, showed acetoacetate variations within a wide range, overlapping with the range for animals with clinical ketosis. Within each of the two materials a statistically significant (P smaller than 0.001) negative correlation (r equal to minus 0.30) was obtained between plasma corticosteroids and log acetoacetate. The lowest corticosteroid and the highest acetoacetate averages were obtained for animals which were within the first month of the lactation cycle. With increasing time post-partum the two components varied inversely, a maximum in corticosteroids coinciding with a minimum in acetoacetate in cows which had calved 2 1/2 to 3 months before the date of sampling. At this stage the mean plasma sugar was about 10 per cent higher than in early lactation. The corticosteroid ranges for different levels of acetoacetate overlapped extensively. Still cows with acetoacetate smaller than or equal to 0.6 mg/100 ml gave significantly higher corticosteroid averages than the rest of the material. But in animals exceeding the 0.6 mg limit no relationship was found between the severity of the ketonaemia and the steroid level. Thus, no difference was obtained between cows with clinical ketosis and animals which were moderately ketonaemic. Some change in adrenal function may be associated with the development of ketonaemic conditions in cows. But no proof has been provided of a direct adrenal involvement in the transformation of a case of subclinical ketosis to the clinical stage.

Acetoacetates↗
PubMed1990

The blue-green blood plasma of marine fish.

1. The blue-green coloration of the blood plasma in some marine fishes, which is attributed to a protein bound tetrapyrrol (biliverdin), is an anomaly in vertebrates. 2. Recent studies have shown that biliverdin not only occurs in many fish, but is also present in the blood of tobacco hornworm, the wings of moth and butterfly, the shell of bird eggs, the serum and egg of frog, the placenta of dog and in the blood of humans suffering from hepatic diseases. 3. In this review, we begin with a historical account of the description of the presence of blue-green blood plasma in fish, and then consider the biochemistry, metabolism, physiology, and the ecological implications of biliverdin in fish. 4. A comparative description of the occurrence of biliverdin in fish and other animals is presented. 5. The mechanism of accumulation of biliverdin in fish blood and its evolutionary significance are also considered. It is suggested that this process may serve as a useful model for further research on bile pigment metabolism in other animals.

Animals↗
PubMed1982

Cytoplasmic blood plasma inclusions in human hepatocytes.

Hepatocellular blood plasma inclusions were demonstrated in conventional formalin-fixed paraffin-embedded liver tissue by the immunoperoxidase technique in 114 out of 197 liver specimens. They were usually round or elliptical in shape, their size varying from a few microns to about 30 microns in diameter. Albumin, fibrinogen, alpha 1-antitrypsin, IgG, IgM, IgA, ceruloplasmin and transferrin were demonstrated in the inclusions, in that order of frequency. A majority were negative with the periodic acid Schiff stain after amylase digestion, but a few were positive. Many of them seemed to correspond to vacuoles in the hepatocytes but some were not seen in HE-stained sections. The inclusions were frequently seen in autopsy liver specimens, but were rare in surgical ones. Most of the inclusions might develop at an agonal stage, probably as a result of hypoxia or circulatory disturbances in the livers.

Adult↗
PubMed2004

Evaluation of an electrolyte analyzer for measurement of ionized calcium and magnesium concentrations in blood, plasma, and serum of dogs.

OBJECTIVE: To evaluate an electrolyte analyzer for measurement of ionized calcium (Ca(i)) and magnesium (Mg(i)) concentrations in blood, plasma, and serum; investigate the effect of various factors on measured values; and establish reference ranges for Ca(i) and Mg(i) in dogs. ANIMALS: 30 healthy adult dogs of various breeds. PROCEDURE: Precision in a measurement series, day-to-day precision, and linearity were used to evaluate the analyzer. The effects of exposure of serum samples to air, type of specimen (blood, plasma, or serum), and storage temperature on sample stability were assessed. Reference ranges were established with anaerobically handled serum. RESULTS: The coefficient of variation for precision in a measurement series was < or = 1.5% for both electrolytes at various concentrations. The Ca(i) and Mg(i) concentrations were significantly lower in aerobically handled serum samples, compared with anaerobically handled samples. The Ca(i) and Mg(i) concentrations differed significantly among blood, plasma, and serum samples. In anaerobically handled serum, Ca(i) was stable for 24 hours at 22 degrees C, 48 hours at 4 degrees C, and 11 weeks at -20 degrees C; Mg(i) was stable for 8 hours at 22 degrees C, < 24 hours at 4 degrees C, and < 1 week at -20 degrees C. In anaerobically handled serum, reference ranges were 1.20 to 1.35 mmol/L for Ca(i) and 0.42 to 0.58 mmol/L for Mg(i). CONCLUSIONS AND CLINICAL RELEVANCE: The electrolyte analyzer was suitable for determination of Ca(i) and Mg(i) concentrations in dogs. Accurate results were obtained in anaerobically handled serum samples analyzed within 8 hours and kept at 22 degrees C.

Analysis of Variance↗
PubMed1992

High-performance liquid chromatographic analysis of amphotericin B in plasma, blood, urine and tissues for pharmacokinetic and tissue distribution studies.

A sensitive and reproducible high-performance liquid chromatographic method was developed to assay ampherotericin B in plasma, blood, urine and various tissue samples. Amphotericin B was isolated from each sample matrix by solid-phase extraction (Bond-Elut). The eluate from Bond-Elut containing amphotericin B was injected onto a reversed-phase C18 column (Waters, mu Bondpak, 10 microns, 300 mm x 3.9 mm I.D.) with a mobile phase of 45% acetonitrile in 2.5 mM Na2EDTA at 1 ml/min. Detection of amphotericin B was by ultraviolet absorption at 382 nm. Blood and tissues were homogenized and extracted with methanol prior to Bond-Elut extraction. The extraction efficiencies of amphotericin B from plasma, blood and tissues were approximately 90, 70 and 75%, respectively. The sensitivity of the assay was less than or equal to 5 ng/ml for plasma, less than or equal to 25 ng/ml for blood, 2.5 ng/ml for urine and 50 ng/g for tissues. The linearity of the assay method was up to 2.5 micrograms/ml for plasma, 5 micrograms/ml for blood, 500 ng/ml for urine and 500 micrograms/g for tissues. The assay was reproducible with an intra-day coefficient of variation (C.V., n = 3) of less than 5% in general for plasma, blood and tissues. The inter-day C.V. of the assay was less than 5% for plasma (n = 5), less than 10% for blood (n = 4) and less than 5% for tissues (n = 3). The overall variability in the urine assay was generally less than 10%. This method has demonstrated significant improvement in the sensitivity and reproducibility in assaying amphotericin B in plasma and especially in blood, urine and tissues. We have employed this assay to compare the pharmacokinetic and tissue distribution profiles of amphotericin B in rats and dogs following administration of Fungizone and ABCD (amphotericin B-cholesteryl sulfate colloidal dispersion), a lipid-based dosage form. In addition, the assay method for plasma and urine samples can also be applied to pharmacokinetics studies of amphotericin B in man.

Amphotericin B↗
PubMedDate not supplied

Influence of different doses of interferon-alpha-2b on the blood plasma levels of 5-fluorouracil.

The blood plasma levels of 5-fluorouracil (5FU) after i.v. administration have been determined without and under the influence of 1, 5 or 9 million units (MU) preadministered interferon (IFN) in patients with gastrointestinal carcinoma. The co-administration of 9 MU IFN causes a doubled increase of the 5FU serum concentrations combined with a statistically significant change of the pharmacokinetics of 5FU for c0, AUC, Vd and Cltot (P < 0.005). A similar effect with distinctly increased serum concentrations could be observed for the preadministration of 5 mU IFN whereby c0 and AUC were elevated significantly (P < 0.05), but not Vd, Cltot and cd. The preadministration of 1 MU IFN also leads to higher plasma levels, but no changes in the pharmacokinetics of 5FU could be calculated (P > 0.05). A linear correlation between the IFN dose and the pharmacokinetic parameters c0 (R = 0.958), AUC0-120 (R = 0.948), Vd (R = 0.941) and Cltot (R = 0.963) of 5FU could be found (P < 0.05), but not for the coefficient of distribution and t1/2el. The results indicate that the pharmacokinetics of 5FU might be influenced by the preadministered IFN dose.

Aged↗
PubMed2000

Comparison between a nucleic acid sequence-based amplification and branched DNA test for quantifying HIV RNA load in blood plasma.

HIV RNA was quantified in blood plasma from 209 patients and in control specimen comparing the NucliSens HIV-1 QT test (Organon Teknika), which is based on the nucleic acid sequence amplification procedure, and the Quantiplex 3.0 test (Bayer), which uses hybridization signal enhancement by branched DNA (bDNA) probes. A highly significant correlation (P=0.01) was found between the two methods with 88% of the samples showing similar results. In cases of discrepant findings, higher virus load was observed with either test (14xNASBA>bDNA; 12xbNDA>NASBA). Differences could neither be related to clinical features nor to divergent virus subtypes. Standard preparations containing 35000 and 222000 copies were quantified with intra-assay coefficients of variation of <20% using both methods. A preparation of 192 copies was measured with lower precision by both tests, yet was detected more reliably by the bDNA method.

Blotting, Western↗
PubMed1988

Antioxidant defenses and lipid peroxidation in human blood plasma.

The temporal disappearance in human blood plasma of endogenous antioxidants in relation to the appearance of various classes of lipid hydroperoxides measured by HPLC postcolumn chemiluminescence detection has been investigated under two types of oxidizing conditions. Exposure of plasma to aqueous peroxyl radicals generated at a constant rate leads immediately to oxidation of endogenous ascorbate and sulfhydryl groups, followed by sequential depletion of bilirubin, urate, and alpha-tocopherol. Stimulating polymorphonuclear leukocytes in plasma initiates very rapid oxidation of ascorbate, followed by partial depletion of urate. Once ascorbate is consumed completely, micromolar concentrations of hydroperoxides of plasma phospholipids, triglycerides, and cholesterol esters appear simultaneously, even though sulfhydryl groups, bilirubin, urate, and alpha-tocopherol are still present at high concentrations. Nonesterified fatty acids, the only lipid class in plasma not transported in lipoproteins but bound to albumin, are preserved from peroxidative damage even after complete oxidation of ascorbate, most likely due to site-specific antioxidant protection by albumin-bound bilirubin and possibly by albumin itself. Thus, in plasma ascorbate and, in a site-specific manner, bilirubin appear to be much more effective in protecting lipids from peroxidative damage by aqueous oxidants than all the other endogenous antioxidants. Hydroperoxides of linoleic acid, phosphatidylcholine, and cholesterol added to plasma in the absence of added reducing substrates are degraded, in contrast to hydroperoxides of trilinolein and cholesterol linoleate. These findings indicate the presence of a selective peroxidase activity operative under physiological conditions. Our data suggest that in states of leukocyte activation and other types of acute or chronic oxidative stress such a simple regimen as controlled ascorbate supplementation could prove helpful in preventing formation of lipid hydroperoxides, some of which cannot be detoxified by endogenous plasma activities and thus might cause damage to critical targets.

Adult↗