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At least 73 records · Page 4Linked to original sources
PubMed1993

Difference in hepatic uptake of tetra- and di-bromosulfophthalein in rat. Role of hydrophobicity, binding to plasma proteins and affinity for plasma membrane carrier protein.

The relative role of hydrophobicity, binding to plasma proteins and affinity for one of the plasma membrane transport proteins in the hepatic uptake of 3,4,5,6-tetra- (BSP) and 3,6-di- (DBSP) bromosulfophthalein was investigated in the rat. In terms of physicochemical characteristics, the two molecules show different pKa values and degrees of hydrophobicity, as determined from the n-octanol:water partition coefficient. In the intact animal, the plasma clearance and the plasma removal rate after a dose of 1.5 mumol/kg i.v. were significantly (P < 0.001) faster for BSP than DBSP, while no difference was found in the plasma distribution volume. The dissociation constant (Kd) of the high affinity binding sites of plasma proteins also differed for the two anions, being significantly lower for BSP than DBSP (0.95 +/- 0.02 vs 1.44 +/- 0.14 microM, P < 0.001). [35S]BSP uptake by liver plasma membrane vesicles was saturable with an apparent Km of 5.20 +/- 0.80 microM, and was competitively inhibited by DBSP (Ki 18.2 +/- 1.2 microM) indicating a common uptake system. The Kd value for binding of the organic anions to purified bilitranslocase, a plasma membrane protein involved in the electrogenic transport of pthaleins, was also significantly lower for BSP than DBSP (1.10 +/- 0.12 vs 3.02 +/- 0.27 microM, N = 3, P < 0.001), indicating a higher affinity of the former ligand for the carrier protein. No difference was observed in the capacity of the high affinity binding sites (32 +/- 3 vs 33 +/- 3 nmol/mg protein, BSP and DBSP, respectively). These data indicate that BSP and DBSP are two different cholephilic organic anions which share a common uptake mechanism, at least partly mediated by bilitranslocase. The greater affinity of BSP than DBSP for the carrier protein may account for the faster plasma disappearance rate of BSP observed in vivo, in spite of the higher plasma protein binding.

Animals↗
PubMed1990

Bovine plasma protein C inhibitor with structural and functional homologous properties to human plasma protein C inhibitor.

Bovine plasma protein C inhibitor was purified; it was then characterized in comparison with human protein C inhibitor. The specific inhibitory activity of the purified inhibitor for bovine activated protein C was 8,500 times that of the inhibitor in plasma. The purified inhibitor showed a single band with Mr 56,000 by SDS-PAGE at pH 7.0, and two bands at pH 8.8, a major one with Mr 56,000 and a minor one with Mr 105,000, under both unreduced and reduced conditions. The pI range of the inhibitor was between 4.4 and 6.1. The Mr of the inhibitor was reduced by treatment with neuraminidase, O-glycanase, and also with glycopeptidase-A, suggesting that the inhibitor has both Asn-linked and Ser/Thr-linked carbohydrate chains. Twenty-seven of the NH2-terminal 49 amino acid residues of the bovine inhibitor, which lacks the first 4 residues from the NH2-terminal amino acid sequence of human inhibitor, were identical to those of the human inhibitor. The bovine inhibitor inhibited bovine and human activated protein C, human thrombin, Factor Xa, Factor XIa, and plasma kallikrein with Ki = 1.0, 5.2, 2.6, 3.0, 1.3 X 10(-8) M, and 4.5 X 10(-9) M, respectively. The inhibitory rates for activated protein C and thrombin were accelerated significantly in the presence of heparin or negatively charged dextran sulfate. However, the acceleration by heparin or dextran sulfate for the inhibition of Factor Xa, Factor XIa, and plasma kallikrein was not significant. The bovine inhibitor did not inhibit human Factor XIIa or plasmin.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1987

Topographical relationships between the monovalent and divalent cation binding sites of des-1-41-light chain bovine plasma protein C and des-1-41-light chain-activated bovine plasma protein C.

The paramagnetic effect of Mn2+ on the longitudinal relaxation rate (T1)-1 of 205Tl+, when both cations are bound to des-1-41-light chain bovine plasma protein C (GDPC) and its activation product, des-1-41-light chain-activated bovine plasma protein C (GDAPC), has been assessed by 205Tl+ NMR spectroscopy. A substantial shortening of the T1 for Tl+ bound to either protein was observed in the presence of Mn2+, an effect not noted upon substitution of Mn2+ with the diamagnetic cation Ca2+, which is known to bind to these proteins in a similar fashion to Mn2+. This paramagnetic effect was employed to estimate distances between the monovalent and divalent cation sites in these proteins, approximately 6.7 +/- 0.2 A with GDPC and 8.3 +/- 0.2 A in GDAPC. These data suggest that a conformational alteration occurs upon activation of GDPC which leads to an increase in the distance between the monovalent and divalent cation sites.

Animals↗
PubMed1996

Activation of renal renin by a protein plasma fraction: a novel enzymatic mechanism.

A 3-fold increase in active renin was found after a kidney cortex extract was incubated with plasma from either normal or nephrectomized rats (0.34 +/- 0.04 to 1.34 +/- 0.08 and 1.60 +/- 0.06 micrograms Angiotensin I/mg tissue/hr, respectively). A plasma protein that activates renal renin was purified 900-fold. Purification of the protein was achieved by a combination of ammonium sulfate fractionation, molecular filtration on Sephacryl S-200 HR and ion-exchange chromatography on Mono Q HR 5/5 associated to an fast performance liquid chromatography (FPLC) system. The protein shows a molecular weight of approximately 54,000 Da. Renin activation was not inhibited by serine protease inhibitors, such as phenylmethyl sulfonylfluoride, aprotinin, soybean trypsin inhibitor and N-tosyl-L-phenylalanine chloromethyl ketone or by the cystein protease inhibitors N-ethylmaleimide and leupeptin. By using enzyme inhibitors, it was found that the activation process is not mediated by kallikrein, plasmin, tonin, cathepsin B or trypsin-like enzymes. From these results, we conclude that there is in circulating plasma a previously unidentified enzyme capable of activating inactive kidney renin. However, the possibility that this protein acts by activating the renin-substrate reaction cannot be dismissed.

Animals↗
PubMed2005

[Plasma protein derivatives].

Plasma protein derivatives produced from human plasma include albumin, blood coagulation factors, immuno globulins, haptoglobin, and c1-inactivator and have been widely used clinically. However, the HIV-tainted blood scandal in which HIV was transmitted to many Japanese patients through blood coagulation factors, must be remembered. The safety of blood products has increased since then in response to that event. Because blood products are provided by volunteer donors, there is a risk of contamination by unknown pathogens and they must be used appropriately. In addition, blood products including plasma derivatives are defined as "special biological products" and regulated by the new Medicine Act. All physicians who prescribe plasma derivatives should understand not only their clinical use but also social expectations and legal regulations.

Biological Products↗
PubMed1979

[Circadian variations of the plasma proteins in the adult male rat under natural synchronisation (author's transl)].

Circadian rhythms of blood total proteins, albumin, alpha 1-, alpha 2-, beta- and gamma-globulins were documented in 80 Wistar SPF adult male rats, synchronized by natural light (06.00-18.00 h) and darkness (18.00-06.00 h) during the month of October 78. Blood was sampled at four fixed time points in the 24 h scale (i.e. 04.00, 10.00, 16.00 or 24.00 h). Total proteins, albumin, alpha 2- and gamma-globulins showed a statistically significant rhythm with a maximum at 04.00 h. The data obtained in anaesthetized rats under artificial synchronization and in man are compared, taking into account that the rat is a nocturnally active rodent. The present work partially confirms the hypotheses of previous chronopharmacological studies, thus e.g. curarizing substances have a mimimum activity when the protein plasma level, especially albumin, is the highest.

Alpha-Globulins↗
PubMed1986

Amitriptyline plasma protein binding: effect of plasma pH and relevance to clinical overdose.

Reversing ventricular ectopy with plasma alkalinization following acute tricyclic antidepressant overdose is a recognized mode of therapy. The mechanism responsible for this effect is unclear. Changes in plasma protein binding of free drug, effects of the sodium ion on the myocardium, and alterations of plasma concentrations of alpha-1-acid glycoprotein may all interact to alter toxicity of tricyclics in overdose. An in vitro investigation using equilibrium dialysis was designed to examine the effect of altering plasma pH on percentage of free amitriptyline at clinical overdose plasma concentrations. A 1973 report on this effect lacked adequate controls and was faulty in experimental protocol. The current investigation used plasma concentrations typically present in amitriptyline overdose, a sensitive gas liquid chromatographic assay to detect total and free drug, and adequate control of plasma pH. The results of two separate experiments demonstrated a significant decrease in percentage of free amitriptyline of 20% over a pH range of 7.0-7.4 (P less than 0.05) and 42% over a pH range of 7.4-7.8 (P less than 0.05). The rate of change in slope in both experiments was not significantly different (P less than 0.01) indicating similar effects of pH change on plasma protein binding of amitriptyline within the two groups.

Amitriptyline↗
PubMed1991

Anthropometric and biochemical assessment of the nutritional state in depression: evidence for lower visceral protein plasma levels in depression.

Severe depression is characterized by anorexia and weight loss, symptoms that could endanger the patient's nutritional state. In order to investigate the nutritional state of depressed patients we determined the following in 113 healthy controls and depressed inpatients: (1) anthropometric variables such as body weight, ideal body weight (IBW), percentage of IBW, mean arm circumference, triceps skinfold thickness and arm muscle circumference, and (2) biochemical parameters such as albumin (Alb), prealbumin (Prealb), and transferrin (Tf). We were unable to detect any differences in the anthropometric parameters between healthy controls, minor and major depressed patients. Depressed patients exhibited significantly lower Alb and Tf levels than healthy controls. The drop in both plasma proteins was highly sensitive (72%) and specific (92%) for melancholia. These results may point towards the existence of a disorder in protein homeostasis or protein malnutrition without a marasmic component.

Adult↗
PubMed1978

[The specific effect of plasma proteins in erythrocyte sedimentation. An analysis of the correlation coefficients between ESR and the concentration of twenty individual plasma proteins in healthy and sick persons, with special reference to myocardial infarction (author's transl)].

1. Spearman's rank correlation coefficient between erythrocyte sedimentation rate and the concentration of twenty individual plasma proteins was determined in 72 persons including 37 patients with recent myocardial infarction. The highest correlation coefficients with ESR could be demonstrated in the following proteins: fibrinogen, alpha-1-acid-glycoprotein, alpha-2-macroglobulin, alpha-1-antitrypsin, coeruloplasmin, Ig M. The closest correlation with ESR was found, when the molar concentrations of fibrinogen, alpha-2-macroglobulin and Ig M were summed up. 2. Subdivision of the examined group of patients according to their diagnosis showed that the degree of correlation with ESR in many plasma proteins essentially depends on the composition of the studied group of patients. The patients with myocardial infarction, with pneumonia and those with neoplasma all showed distinctly different patterns of correlation. These obviously reflect underlying changes in the concentrations of the studied proteins, that seem to be specific to the respective disease. 3. In 4 patients with myocardial infarction the changes in plasma protein concentrations together with ESR were followed over a period of 26 days after the infarction.

Blood Proteins↗
PubMed2006

Effects of storage time and exogenous protease inhibitors on plasma protein levels.

Plasma biomarker analysis requires intact unbiased starting material. We analyzed the effects on plasma protein profiles of protease inhibitor cocktails and preprocessing storage. Plasma from 12 healthy subjects collected with and without protease inhibitors was prepared immediately and after 2 hours of room temperature storage. The samples were analyzed by a multiplexed enzyme-linked immunosorbent assay that captured 99 chemokines and cytokines. Unsupervised hierarchical analysis clustered the samples into 4 groups; one composed predominantly of samples processed immediately, another of samples processed after 2 hours, and the remaining two were a mix of immediate and 2-hour samples. The mixed and immediate group protein profiles were similar. However, among the immediate and 2-hour samples, the levels of 37 factors differed significantly: all were greater after 2 hours. The dramatic changes in protein levels during storage were independent of protease inhibitors and are likely due to cytokine production and/or release by leukocytes and platelets.

Blood Preservation↗
PubMed1983

Pharmacokinetics of ibuprofen in man--III: Plasma protein binding.

Plasma protein binding of ibuprofen was measured by equilibrium dialysis on 406 plasma samples collected from 15 normal volunteers following doses of 400, 800, and 1200 mg of ibuprofen as tablets (N = 102, 100, 104, respectively) and 420 mg as an aqueous solution (N = 100). Individual subject bound concentration at dialysis equilibrium (Cbd) vs. free concentration at dialysis equilibrium (Cfd) were well fitted via computer to the Scatchard equation with one class of binding sites. The binding capacity averaged 1231 microM (range 848-1658 microM), and the association constant averaged 1.76 X 10(5) M-1 (range 1.15 X 10(5) to 2.73 X 10(5) M-1). Distributional analysis was performed on the free fraction (fd) and bound/free ratios (Cbd/Cfd = 1/fd-1) at dialysis equilibrium for each treatment. Using pooled data of all four treatments, distributional analysis was also performed on the free fractions (f) and bound/free ratios (Cb/Cf = 1/f-1) corresponding to the plasma drug concentrations in blood as it was withdrawn from the subjects. The bound/free ratios were normally distributed, whereas the distributions of the free fractions were skewed towards higher values.

Adult↗