- General Drug Summary
- Drug Name
- Human Serum Albumin
- Description
- Human serum albumin isolated from expired blood plasma
- Also Known As
- Serum albumin precursor
- Categories
- Serum substitutes
- Structure
- Summary In Neonatal Jaundice
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5 record(s) for Human Serum Albumin Effective in Inducing Remission in Neonatal Jaundice.
- PMID
- Drug Name
- Efficacy
- Evidence
- 20047841
- Human Serum Albumin
- Effective in Inducing Remission
- Clinical Trial
- Summary
- Facilitate the photochemical change of bilirubin is evolutionarily selected in response to Neonatal jaundice in humans.
- (EZ)-Cyclobilirubin formation from bilirubin in complex with serum albumin derived from various species. Journal of photochemistry and photobiology. B, Bio, 2010 Feb 12 [Go to PubMed]
- We determined the specificity of photochemical changes of bilirubin in complex with serum albumin from various species. There were no general trends in the configurational photoisomerizations of (ZE)-bilirubin/(ZZ)-bilirubin and (EZ)-bilirubin/(ZZ)-bilirubin associated with the albumins from various species as compared to those associated with human serum albumin. The absorbance spectra of bilirubin in complex with albumins from various species differed, indicating that the three-dimensional structures of (ZZ)-bilirubin bound to the various serum albumins, which are substrates of (ZE)- and (EZ)-bilirubin, differ among species. The rates of conversion of the (EZ)-bilirubin isomer into the structural cyclobilirubin isomer were similar for the albumins of chicken, rat, rabbit, dog, bovine, and pig, and were significantly slower than the rate for human serum albumin. This suggests that the three-domain human albumin has evolved to allow ready conversion of (EZ)-bilirubin to (EZ)-cyclobilirubin. Cyclobilirubin fomation in a bilirubin-alpha-fetoprotein solution was much lower than that in a bilirubin-human serum albumin solution. It is believed that the ability of human serum albumin to facilitate the photochemical change of bilirubin was evolutionarily selected in response to neonatal jaundice in humans.
- 18553870
- Human Serum Albumin
- Effective in Inducing Remission
- Review
- Summary
- The effect is a delay of the decrease of free bilirubin concentration, or even a temporary increase.
- An immobilized enzyme reactor for the detoxification of bilirubin. Biotechnology and bioengineering, 1986 Oct [Go to PubMed]
- An immobilized enzyme reactor has been developed for the degradation of bilirubin as a potential treatment for neonatal jaundice. It utilizes the enzyme bilirubin oxidase from Myrothecium verrucaria, which in the presence of molecular oxygen converts bilirubin to biliverdin and other products that are much less toxic than bilirubin. Bilirubin oxidase was covalently attached to agarose beads using cyano transfer activation. Forty percent of the specific activity of bilirubin oxidase was retained after immmobilization, and preparations with 20 units of enzymatic activity per gram of drained wet weight of gel were obtained. The stability of bilirubin oxidase at pH 7.4 and 37 degrees C was improved fivefold by immobilization. A 15-mL column containing immobilized bilirubin oxidase, through which a 37 degrees C solution of 332muM bilirubin and 450muM human serum albumin in 0.05M phosphate buffer (pH 7.4) was passed at 1 mL/min, converted more than 60 percent of the bilirubin per pass. The substrate specificity ofthe enzyme and the small volume of the reactor are important characteristics for this clinical application where it is desirable to remove only one compound from the blood and to minimize the volume of blood in the extracorporeal circuit. This reactor, by detoxifying the jaundiced infant's blood of bilirubin, would eliminate the risks associated with the use of donor blood as is done currently in treating severe neonatal jaundice.
- 557276
- Human Serum Albumin
- Effective in Inducing Remission
- Clinical Trial
- Summary
- The effect is a delay of the decrease of free bilirubin concentration, or even a temporary increase.
- Bilirubin displacing effect of stabilizers added to injectable preparations of human serum albumin. Acta paediatrica Scandinavica, 1977 Mar [Go to PubMed]
- Stabilizers added to preparations of human serum albumin before heat treatment were tested for bilirubin displacing effect, using the peroxidase method. It was found that N-acetyltryptophan and sodium caprylate displace bilirubin from its complex with human serum albumin in vitro. The quantitative findings were used for a rough estimate of the effect of these substances on the free bilirubin concentration in blood plasma, expected when stabilized albumin preparations are given intravenously for prevention of kernicterus. The calculated effect is a delay of the decrease of free bilirubin concentration, or even a temporary increase. Sodium mandelate displaces less strongly.
- 7208154
- Human Serum Albumin
- Effective in Inducing Remission
- Clinical Trial
- Summary
- The effect is a delay of the decrease of free bilirubin concentration, or even a temporary increase.
- Phototherapy-induced covalent binding of bilirubin to serum albumin. Pediatric research, 1980 Dec [Go to PubMed]
- Bilirubin displays a detectable fluorescence emission only when it is complexed with serum albumin, whereas free bilirubin has a very low fluorescence yield. Actually, nearly complete disappearance of bilirubin emission was obtained when the unirradiated human serum albumin-bilirubin complex was precipitated with acetone to extract the pigment; complete removal of protein-bound bilirubin (as monitored by fluorescence spectroscopy) was achieved by repeating the acetone extraction after incubation of the complex in the phosphate buffer, pH 7.4, containing 7 M guanidinium chloride; the latter compound causes on extensive unfolding of protein molecules. On the other hand, in the case of irradiated solutions, even after denaturation of the protein with 7 M guanidinium chloride, a detectable amount of bilirubin-type fluorescent material was found to be associated with albumin. This finding clearly shows that bilirubin and/or some photoproduct underwent in part a photoinduced covalent binding with human serum albumn. Fragmentation of the bovine albumin polypeptide chain according to the procedure detailed in the experimental section yielded only one peptide-containing material fluorescent in the 530 nm region. This fact underlines the selective nature of the photobinding reaction. The amino acid composition of the isolated peptide is shown in Table 2; the composition is closely similar with that found for peptide 187-397 of native bovine serum albumin. In the case of the jaundiced babies who were subjected to phototherapy, we were able to demonstrate that only after 7 to 9 hr of exposure to light a detectable amount of bilirubin-type fluorescent material was present even at the end of the serum treatment with acetone and guanidinium chloride (see Fig. 1; Table 1). Fractional precipitation of the serum proteins by addition of controlled amounts of ammonium sulphate showed that the fluorescent material was present only in the albumin fraction. The photoadduct disappeared about 15 to 20 days after the phototherapy had ben discontinued. This period of time represents the natural turnover period of human serum albumin.
- 963887
- Human Serum Albumin
- Effective in Inducing Remission
- Review
- Summary
- The effect is a delay of the decrease of free bilirubin concentration, or even a temporary increase.
- The interactions between iophenoxic acid, iopanoic acid, bilirubin and human serum albumin as studied by fluorescence and Sephadex gel filtration. Clinica chimica acta; international journal of cli, 1976 Sep 6 [Go to PubMed]
- Iophenoxic acid increases the fluorescence of bilirubin bound to human serum albumin at drug/albumin molar ratios lower than 1, while iopanoic acid decreases it. The fluorescence enhancement results probably from a change in the fluorescence efficiency due to an iophenoxic acid-induced conformational change in the albumin, which in turn causes displacement of bilirubin from the protein. Iophenoxic acid does not affect the high-affinity bilirubin binding site of albumin. Therefore any enhancement in bilirubin fluorescence caused by the drug indicates that bilirubin is bound to the low-affinity binding sites of albumin. The use of iophenoxic acid in the determination of the extent of saturation of the high-affinity bilirubin binding site of albumin may be of value in the clinical management of infants with neonatal jaundice.
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3 record(s) for Human Serum Albumin Effective in Maintaining Remission in Neonatal Jaundice.
- PMID
- Drug Name
- Efficacy
- Evidence
- 10768487
- Human Serum Albumin
- Effective in Maintaining Remission
- Clinical Trial
- Summary
- Monomeric human serum albumin without organophilic ligands exerted a protective effect on NO synthase in bilirubin-containing membrne particles
- Effect of bilirubin on the activity and thermokinetic characteristics of brain (synaptosomal) membrane NO synthase. cell biology, 2000 [Go to PubMed]
- NO synthase activity was found in the plasma (synaptosomal) membrane particles isolated from the homogenate of adult rat brain (without cerebellum) under conditions preventing the protease attack and formation of reactive oxygen species. The NO synthase discovered exhibited some properties of a neuronal constitutive integral membrane enzyme and was inhibited by N-nitro-L-arginine. NO synthase activity decreased when bilirubin entered the synaptosomal membrane in vitro. Bilirubin caused the shift of the transition temperature in the temperature dependence of NO synthase activity in Arrhenius plots. The incorporation of bilirubin into synaptosomal membranes resulted in an increase in the apparent activation energy for NO synthase within a temperature range of 10-30 degrees C. The membrane NO synthase was susceptible to the photodynamic effect of membrane-bound bilirubin molecules. Monomeric human serum albumin without organophilic ligands exerted a protective effect on NO synthase in bilirubin-containing membrne particles.
- 1164793
- Human Serum Albumin
- Effective in Maintaining Remission
- Clinical Trial
- Summary
- Analysis in the presence of excess human serum albumin solution appears to reflect the bilirubin tightly bound to albumin and the total serum bilirubin.
- in the jaundiced neonate. Clinical chemistry, 1975 Oct [Go to PubMed]
- We report a fluorometric technique for determination of albumin-titratable bilirubin in the jaundiced neonate. Although bilirubin alone has very little native fluorescence, considerable emission is observed in the presence of albumin under acid conditions. Analysis of the plasma sample alone and in the presence of excess human serum albumin solution appears to reflect the bilirubin tightly bound to albumin and the total serum bilirubin, respectively. The difference between these two values has been designated as"
albumin-titratable bilirubi"
. Where the concentration of albumin-titratable bilirubin is considerable, a typical saturation effect is observed. In samples where the circulating bilirubin is strongly bound to endogenous alumin, no change in fluorescence is seen when exogenous albumin is added. Results correlate well with the clinical picture.
- 7136621
- Human Serum Albumin
- Effective in Maintaining Remission
- Clinical Trial
- Summary
- Infusion of both HSA preparations during phototherapy provides an immediate protection.
- Comparison between two preparations of human serum albumin in treatment of neonatal hyperbilirubinaemia. Acta paediatrica Scandinavica, 1982 Jan [Go to PubMed]
- Thirty-six newborn infants with normal birth weights and with uncomplicated hyperbilirubinaemia, treated with light, were studied. At onset of phototherapy the infants received intravenously 1 g human serum albumin (HSA) per kg body weight as a 9% solution. Two different preparations of HAS were used and compared. One of these, HSAI, contained sodium caprylate and N-acetyltryptophan, 5 mmol/l of each, as stabilizers. HSAII contained only caprylate, 5 mmol/l. Nineteen infants received HSAI and seventeen infants HSAII. The reserve albumin for binding of bilirubin, measured by the [14C] MADDS method, was low in both preparations in vitro. During the infusion, the serum concentrations of albumin and reserve albumin increased and the serum unconjugated bilirubin concentration decreased, resulting in a fall in the index of plasma bilirubin toxicity in all infants. After completion of the infusion, the serum concentrations of albumin and reserve albumin declined, and a slight rise in index occurred. The increase inthe serum reserve albumin concentration was markedly higher during infusion of HSAII than of HSAI. It is concluded that infusion of both HSA preparations during phototherapy provides an immediate protection against bilirubin encephalopathy. HSAI is inferior to HSAII, probably due to its content of N-acetyltryptophan.
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1 record(s) for Human Serum Albumin NA in Neonatal Jaundice.
- PMID
- Drug Name
- Efficacy
- Evidence
- 8903413
- Human Serum Albumin
- NA
- In Vitro Study
- Summary
- Studies of binding of UCB to human serum albumin (HSA) showed marked diminution of UCB-binding affinity as albumin and chloride concentrations increased.
- New concepts in bilirubin and jaundice: report of the Third International Bilirubin Workshop, April 6-8, 1995, Trieste, Italy. Hepatology (Baltimore, Md.), 1996 Nov [Go to PubMed]
- The workshop covered three major areas: Unconjugated bilirubin (UCB) chemistry and physical chemistry; UCB transport and intracellular trafficking; and evaluation and therapy of neonatal and congenital hyperbilirubinemias. Findings of studies in the chemistry and physical chemistry area were as follows. (1) Nuclear magnetic resonance (NMR) studies of highly enriched 13COOH mesobilirubin in water-dimethyl sulfoxide systems indicated that the pKa values of the carboxyl groups are 4.2 and 4.9, respectively. This finding differs from some reports that suggest that the two pKa values in aqueous systems are near or above pH 7.0. (2) Contrasting views of the hydrophobic interactions of UCB with bile salts were presented: one suggested that multiple bile salt monomers bind to one UCB molecule; the other suggested that UCB binds to the nonpolar surface of helical bile salt micelles. (3) Structures were proposed for the varied calcium and copper bilirubinate salts formed at various pH values and cation/UCB ratios. (4)Studies of binding of UCB to human serum albumin (HSA) showed marked diminution of UCB-binding affinity as albumin and chloride concentrations increased. (5) A unique UCB derivative, bilirubin-C10-sulfonic acid, was identified as the major bile pigment in bullfrog bile. (6) New methods were presented for removal of impurities from preparations of bile salts and UCB. Findings of studies in the transport area were as follows. (1) Four putative basolateral and two putative canalicular hepatocytic transporters of UCB and related organic anions were described. Special emphasis was given to the adenosine triphosphate (ATP)-dependent canalicular multi-specific organic anion transporter that is defective in three strains of mutant rats with congenital conjugated hyperbilirubinemia. (2) The roles of the classical and newer molecular biological approaches to identification of these transporters were contrasted, and their limitations were discussed. (3) The relative roles of the multiple carriers in UCB transport underdifferent conditions and substrate concentrations were discussed. (4) Cytosolic UCB-binding proteins (e.g., ligandin) were shown to promote transcellular movement of UCB by solubilizing and transporting the pigment in the aqueous phase while limiting binding of UCB to the relatively immobile membranes of cell organelles. (5) Mechanisms were presented for translocation of UDP-glucuronic acid (UDPGA) into the lumenal location of UDPGA transferase in the endoplasmic reticulum, as well as the enhancement of this process by N-acetyl-glucosamine. Studies in the neonatal and congenital jaundice area were as follows. (1) Criteria were reviewed for initiating treatment of neonatal jaundice, emphasizing the primacy of serum bilirubin levels, gestational age, and hemolysis as risk factors for kernicterus. (2) New methods were presented for frequent, automated monitoring of serum bilirubin levels and breath CO levels as an index of rates of formation of UCB from heme. (3) The current status and limitations of new approahes to treatment of severe unconjugated hyperbilirubinemia were discussed: hepatocyte transplantation and gene therapy, still in the stage of development in animal models, have provided only partial and temporary relief of hyperbilirubinemia; extracorporeal liver assist devices have had some success in initial human studies; and inhibition of heme oxygenase (HO) with metalloporphyrins, especially tin mesoporphyrin, which markedly decreases bilirubin production for prolonged periods, is a new alternative to phototherapy. (4) The ontogeny of the two HO isozymes was contrasted in the liver, spleen, kidney, and lung.
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1 record(s) for Human Serum Albumin Not Effective to Patients in Neonatal Jaundice.
- PMID
- Drug Name
- Efficacy
- Evidence
- 1255322
- Human Serum Albumin
- Not Effective to Patients
- Randomized Controlled Trial
- Summary
- Beneficial effects of albumin therapy was apparent only in those infants with low RABC as determined by the sephadex gel filtration technique.
- Variance in albumin loading in exchange transfusions. The Journal of pediatrics, 1976 Apr [Go to PubMed]
- To assess the rationale of albumin priming prior to exchange transfusions, 42 hyperbilirubinemic infants who required exchange transfusions were randomly assigned to one of two groups. Group I consisted of 15 infants who were given intravenously 1 gm/kg of salt-poor human serum albumin one hour before the exchanges. Group II, which consisted of 27 infants, received simple exchanges. No statistical differences were found in variations in reserve albumin-binding capacity, bilirubin, albumin, or red cell bilirubin at pre and one-hour post albumin infusion in the primed infants. The amount of bilirubin removed per kilogram is directly correlated to plasma bilirubin concentration (r=0.87). No significant difference in efficiency on bilirubin removal was seen between the two groups. Beneficial effects of albumin therapy was apparent only in those infants with low RABC as determined by the sephadex gel filtration technique.