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PubMed1994

Preliminary observations on plasma fibrinogen and plasma protein concentrations and on plasma protein:fibrinogen ratios in clinically healthy buffaloes.

The plasma fibrinogen concentration, the total plasma protein concentration and the plasma protein to fibrinogen ratio (PP:F) were determined in clinically healthy Nili Ravi buffaloes. The plasma fibrinogen concentrations in calves, lactating and non-lactating buffaloes were 513 +/- 62, 615 +/- 90 and 544 +/- 74 mg/dl, respectively, and were statistically different (p < 0.05). Total plasma protein concentrations in these animals were 7.15 +/- 0.28, 9.32 +/- 0.53 and 8.79 +/- 0.58 g/dl. PP:F for all animals was between 11 and 19. Fibrinogen levels were positively correlated with plasma protein (r = 0.59) and negatively correlated with PP:F (r = -0.59).

Animals↗
PubMed1989

Two-dimensional electrophoresis of the plasma proteins of alpacas and llamas: genetic polymorphism of alpha 1B-glycoprotein and three other proteins.

Plasma samples of alpacas and llamas were analysed by a simple method of two-dimensional (2-D) agarose gel (pH 8.6)-horizontal polyacrylamide gel (pH 9.0) electrophoresis, followed by general protein staining of gels. Genetic polymorphism in both species is described for alpha 1B-glycoprotein (alpha 1B) and three other unidentified proteins designated prealbumin (Pr), postalbumin 1 and 2 (Pa1 and Pa2). alpha 1B was identified by cross-reactivity with antisera for human and pig alpha 1B. Altogether, two alleles of Pr, two of Pa1, five of alpha 1B and three of Pa2 are described. Most of the alleles were present in alpacas and llamas. Alpacas showed a high degree of polymorphism at all four loci. Llamas showed considerable polymorphism at only the Pa1 and Pa2 loci. The theoretical probability of exclusion (PE) of an incorrectly assigned parent was estimated to be about 80% in each species by typing for the six polymorphic plasma proteins reported so far in these species. The given method of 2-D electrophoresis revealed no fixed differences in protein mobilities that discriminate between llamas and alpacas.

Alleles↗
PubMed1990

Tianeptine binding to human plasma proteins and plasma from patients with hepatic cirrhosis or renal failure.

1. The binding of tianeptine to human plasma, isolated plasma proteins, red blood cells and to plasma from patients with cirrhosis or renal failure was studied in vitro by equilibrium dialysis. 2. Tianeptine is highly bound to plasma (95%) at therapeutic concentrations (0.3-1 microM). No saturation of the binding sites was seen. 3. Human serum albumin (HSA) was shown to be mainly responsible for this binding (94%) with a saturable process characterized by one binding site with a moderate affinity (Ka = 4.2 x 10(4) M-1) and a non-saturable process with a low total affinity (nKa = 1.2 x 10(4) M-1). 4. Like many basic and amphoteric drugs, tianeptine showed a saturable binding to alpha 1-acid glycoprotein (AAG) with one site and a moderate affinity (Ka = 3.7 x 10(4) M-1). Its binding to lipoproteins and red blood cells (RBC) was weak and non-saturable. Over the range of therapeutic drug concentrations (0.3-1 microM), the unbound fraction in blood remains constant (4.5%). 5. Interactions were studied using non-esterified fatty acids (NEFA) at pathological concentrations; they altered tianeptine binding to plasma and to isolated HSA. Tianeptine seems to bind to a HSA site different from sites I (warfarin) and II (diazepam), but close to site II. It also shares the only basic-site on AAG. However, at therapeutic drug concentrations (0.3-1 microM), not all of these interactions occur. 6. The binding of tianeptine varied according to HSA, AAG and NEFA concentrations both in patients and healthy subjects. In patients with chronic renal failure having high NEFA concentrations the unbound fraction of tianeptine (fu) increased from 0.045 to 0.153 compared with normal (P less than 0.001). In cirrhotic patients, with relatively low HSA concentrations, the fu of tianeptine increased from 0.045 to 0.088 compared with normal (P less than 0.01). 7. Multiple regression analysis of all of the data indicated that the fu of tianeptine was related significantly to HSA, NEFA and AAG concentrations, with a particularly strong correlation with NEFA concentrations. Therefore, variation of HSA and NEFA concentrations in patients on maintenance therapy may cause an increase of tianeptine fu.

Adult↗
PubMed1998

Incorporation of urea nitrogen into fecal protein and plasma protein amino acids in elderly human volunteers after ingestion of lactic acid bacteria.

Health effects of fermented milks have been associated with the metabolic activity of lactic acid bacteria in the gastrointestinal tract. It has been proposed that an increased excretion of urea nitrogen via microbial protein may decrease the workload on kidneys and liver. Therefore, a study was carried out in healthy elderly human subjects to investigate the incorporation of [15N2]urea nitrogen into plasma and fecal proteins and amino acids. Over a period of 10 d 13 healthy elderly subjects ingested daily a freeze-dried microbial preparation which contained different genera of lactic acid bacteria and is used to produce fermented milk products. One of the strains was originally isolated from stool samples of elderly people from the Caucasus region (Lactobacillus plantarum). No stimulation of fecal protein-nitrogen excretion and no increase in 15N-abundances in fecal protein was measured following the administration of the viable microbial preparation and a [15N2]urea bolus. Tentatively, it was concluded that this may have been caused by the inability of the microbial culture to survive the gastro-intestinal passage and (or) by the absence of additional fermentable carbohydrates in the diet as energy source for bacterial protein synthesis in the large intestine. However, using a highly sensitive GC-C-IRMS method we observed a significant incorporation of 15N into plasma protein amino acids. 15N-Enrichments in single amino acids were found according to their participation in transamination reactions. The slight enrichment of lysine which is not transaminated in mammalian tissues may indicate a microbial synthesis and absorption of bacterial lysine.

Aged↗
PubMed1995

Effects of storage on the binding of carboplatin to plasma proteins.

Plasma ultrafiltrates are routinely used in pharmacokinetic studies of carboplatin. Experiments were performed to detect and quantitate artifactual decreases in the platinum concentration of ultrafiltrates prepared from plasma samples stored at -20 degrees C and -70 degrees C. Carboplatin was added to anticoagulated, whole human blood to produce a 20 microgram/ml concentration. Plasma produced from the blood was stored frozen at either -20 degrees C or -70 degrees C. Aliquots from each storage condition were thawed and ultrafiltered once a week for up to 100 days. Platinum concentrations in ultrafiltrates and plasma were determined by flameless atomic absorption spectrometry. There was no loss of ultrafilterable platinum in plasma samples stored at -70 degrees C, whereas there was a steady decrease in free platinum concentration in ultrafiltrates prepared from plasma samples stored at -20 degrees C. These results imply that pharmacokinetic studies of carboplatin should use ultrafiltrates prepared immediately or that plasma for such studies should be stored at -70 degrees C. Storage of carboplatin-containing plasma at -20 degrees C and subsequent ultrafiltration is not acceptable, because measurement of platinum in such ultrafiltrates will be artifactually low.

Blood Preservation↗
PubMed1951

Conversion of plasma protein to tissue protein without evidence of protein breakdown; results of giving plasma protein labeled with carbon 14 parenterally to dogs.

Labeled plasma proteins obtained from donor dogs, previously fed epsilon-C(14)-dl-lysine, have been given intravenously to recipient dogs. The disappearance of labeled globulin from the plasma at a rate considerably faster than albumin has been confirmed. Evidence suggesting that the mass of protein in solution in the extravascular, extracellular fluid is approximately equal to the plasma proteins in circulation has been derived from a study of the dilution of labeled plasma protein by repeated injections of non-labeled plasma protein. In a period of 7 days the transfer of C(14) from plasma to tissue proteins amounted to between 30 and 40 per cent of the activity in the labeled plasma protein injected intravenously. The conversion was accompanied by a very small loss of activity in the urine and expired air and the activity remained in the lysine residue of the liver and probably of other tissues. The data presented favor the view that plasma proteins are utilized in the body economy after partial catabolism within the cell area and provide no evidence of complete breakdown to the amino acid level.

Amino Acids↗
PubMed2005

Effects of total plasma protein concentration on plasma sodium, potassium and chloride measurements by an indirect ion selective electrode measuring system.

OBJECTIVE: Ion selective electrodes (ISE) measure electrolytes by two different technologies, direct and indirect. We wished to investigate the effect of total plasma protein concentration on the plasma sodium, potassium and chloride measurements by indirect ISE compared with measurements by direct ISE. METHODS: The evaluation of the objective was performed in a tertiary care hospital on patient blood samples sent to the pathology laboratory for general chemistry analysis. To determine the degree of difference between the two ISE measurements, 195 lithium heparin plasma samples were measured and the results were separated into three groups (65 samples in each group) depending on the protein concentration (e.g. total plasma protein concentration less than, greater than and within the reference range between 62-83 g/L). The samples were analysed over a 40 day period on a Hitachi Modular ISE system - indirect ISE (Roche Australia) and Bayer Rapidlab 865 Blood Gas Analyser - direct ISE (Bayer Diagnostics, Australia). RESULTS: Using indirect ISE, low plasma protein concentrations caused a 'pseudohyper' effect in all 3 analytes and a 'pseudohypo' effect with high plasma protein concentrations. The variation in total protein concentration had the greatest effect on plasma sodium measurement. The relationship was non-linear and no accurate predictive value could be calculated for the plasma electrolytes with changes in plasma protein concentrations. CONCLUSIONS: The plasma sodium, potassium and chloride measurements are effected by changes in plasma protein concentration when measured by indirect ISE systems. Clinicians must be aware that differences exist between the ISE technologies and in border-line clinical situations, the direct ISE systems provide a more accurate estimate of plasma sodium, potassium, chloride, anion gap, osmolality and strong ion difference calculations, and should be used for clinical decision-making.

Journal Article↗
PubMedDate not supplied

Influence of preoperative intravenous nutrition upon hepatic protein synthesis and plasma proteins and amino acids.

The influence of 3 and 7 days of preoperative intravenous nutrition (IVN) on the capacity for protein synthesis in liver and on concentrations of plasma proteins and amino acids were investigated in patients with gastrointestinal malignancy. Thirty patients with gastrointestinal neoplasms who had lost more than 5 kg of weight over 3 months were randomized into three groups to receive preoperatively: (a) no IVN, (b) IVN for 3 days (0.18 gN/kg/day as amino acid; 30 kcal/kg/day as glucose), or (c) IVN for 7 days. Free access to a hospital diet was available to all patients including 10 patients who had not lost weight who served as controls. In the three groups of patients who had lost weight, median transferrin and fibronectin were lower than for controls, whereas other proteins and amino acids were comparable. After feeding, samples of liver were obtained peroperatively and the potential rates of protein synthesis were calculated from the in vitro incorporation of (14C)-leucine, into protein. Preoperative IVN significantly increased the potential rate of protein synthesis in liver after 3 days. Plasma amino acids were comparable with controls whereas in the unfed-group concentrations suggested utilization of alanine and breakdown of muscle. Three days of IVN also increased plasma fibronectin and IgA but increases of prealbumin, IgM, and complement C3 were only significant in the group fed for 7 days. On the 7th postoperative day plasma proteins were decreased similarly in each group. This study shows that concentrations of several plasma proteins, in preoperative patients reflect net rates of hepatic protein synthesis and are susceptible to depletion during starvation and repletion by 3 or 7 days of IVN.

Aged↗
PubMed2005

Immunodepletion of albumin for two-dimensional gel detection of new mouse acute-phase protein and other plasma proteins.

Immunodepletion of albumin to improve the 2-D gel resolution of human plasma proteins has recently been described. With the importance of mouse models in many studies in which serum or plasma is often analyzed, we have adopted this approach to immunoprecipitate mouse albumin and evaluated its effectiveness for 2-D separation of mouse plasma proteins. Purified polyclonal antibodies against mouse albumin were effective depleting intact albumin as well as its numerous fragments from mouse plasma samples. Removal of albumin resulted in better resolution of mouse plasma proteins. Three proteins, alpha2-macroglobulin, coagulation factor XII, and hemopexin, that were previously either undetectable or poorly resolved, were identified from albumin-depleted 2-D gels by peptide mass fingerprinting. Albumin depletion also led to partial loss of several other proteins such as clusterin and gelsolin. This loss can be attributed to the interaction with albumin itself because the specificity of the antibody was demonstrated by Western blot. When applying this method to the 2-D separation of plasma from inflamed mouse induced by cutaneous burn injury with superimposed Pseudomonas aeruginosa infection, the upregulation of inter alpha-trypsin inhibitor heavy chain 4 (ITIH4) and hemopexin was unambiguously detected along with other mouse acute-phase proteins (APP), including haptoglobin and serum amyloid A. Based on the significant increase of ITIH4, we propose that this protein is a new member of mouse APP that are upregulated during the inflammatory response.

Acute-Phase Proteins↗
PubMed1990

[Problems in standardization of the immunochemical detection of plasma proteins. I. International reference standards for plasma proteins. II. Immunochemical relation of measurement signals and values].

When the results of plasmaprotein determination--dependent on the reagents, methods and other factors--are expressed in international units (IU) a better comparison of the results between different labs is possible. By this means and using the corresponding reference values and reference intervals the reliability of the interpretation of laboratory data will increase. The situation regarding the WHO IRP's for plasma proteins (approx. 20 parameters) and the relation from IU to mg in the reagents of the Behringwerke AG are reported. The overlability of WHO IRP's has not allowed yet to achieve an optimal standardization of the immunochemical methods for measurement of plasma proteins. This depends especially on the complexity of the antigen-antibody reaction. The relationship between the measured signal and the hence obtained value will be discussed in details in the second part of this paper. Hereby especially the reciprocal interdependence between physicochemical properties of proteins and the deriving immunochemical behaviour as well as the dependence of the results from the quality of the antibodies-containing reagents are also considered. Possible solutions for a better control system of the plasma protein determination by using the so called master calibrators as internal support for validation will be presented. Furthermore, general immunochemical postulates and rules for optimization of the standardization of plasma protein determination will be proposed and discussed.

Antigen-Antibody Complex↗