Showing papers on "Serum albumin published in 1969"
TL;DR: Conjugation of peroxidase, glucose oxidase, tyrosinase and alkaline phosphatase to human immunoglobulin-G, human serum albumin, sheep antibody and rabbit antibody was carried out with glutaraldehyde to characterize the antibodies after immunoelectrophoresis.
1,453 citations
TL;DR: In general, palmitate and palmitoleate were bound more tightly than oleate, linoleate, stearate, or myristate, and muchMore tightly than laurate.
453 citations
202 citations
TL;DR: These effects may be important for understanding the increased blood levels of certain plasma α and β globulins that occur in vivo in mammals after many forms of injury and may serve as a useful model for furthering the understanding of the influence of hormones and amino acids on protein synthesis.
164 citations
TL;DR: Distribution of values of serum calcium, serum magnesium, serum inorganic phosphorus, blood urea, total serum proteins, serum albumin, and serum alkaline phosphatase has been studied in 278 women and 298 men who upon careful examination have been found to be in good health.
152 citations
TL;DR: Experiments demonstrated that digitoxin was almost exclusively bound by albumin, and the marked difference in avidity of digitoxin and digoxin for serum albumin is reflected by the higher plasma concentrations, lower rate of urinary excretion, and longer half-time of Digoxin when these compounds are administered to man.
Abstract: Tritium-labeled digitoxin, digitoxigenin, digoxin, and digoxigenin of established purity and chemcal authenticity were used to study the binding of these compounds to human plasma proteins. 97% of digitoxin in plasma was nondialyzable. Continuous flow paper electrophoresis of plasma containing digitoxin and dialysis experiments in which human serum albumin competed for the glycoside with plasma or plasma protein fractions demonstrated that digitoxin was almost exclusively bound by albumin. Equilibrium dialyses revealed that the interaction was characterized by a single binding site on the albumin molecule and an association constant of 9.62 x 10(4) liter/mole at 37 degrees C. At 1 degrees C the association constant was 4.64 x 10(4) liter/mole. The interaction therefore was endothermic; the gain in enthalpy of 3.5 kcal/mole and the free energy change of - 7.06 kcal/mole was derived from a large change in entropy of 33.8 cal/mole per degrees K. The direction of these thermodynamic changes suggested the formation of a hydrophobic bond between digitoxin and albumin. Quenching of the fluorescence of albumin by digitoxin indicated that the conformation of albumin was altered by the binding process.Digitoxigenin, its mono- and didigitoxosides, digoxin, and digoxigenin competed with digitoxn for its binding site on albumin. The affinity of the mono- and didigitoxosides for the site was equal to that of digitoxin, but that of digitoxigenin was only one-third as great. The ability of the digitoxose residues of the glycosides to enhance binding to albumin was also observed with digoxin, which was more extensively bound by the protein than digoxigenin. At concentrations of 2 mug/ml or less in plasma, only 23% of digoxin was bound. Albumin, which interacted with digoxin with an apparent association constant of 9 x 10(2) liter/mole at 37 degrees C, was entirely responsible for the binding. Lowering the temperature from 37 degrees to 1 degrees C decreased the fraction of digoxin bound to albumin by two-thirds. The marked difference in avidity of digitoxin and digoxin for serum albumin is reflected by the higher plasma concentrations, lower rate of urinary excretion, and longer half-time of digitoxin as compared to those of digoxin when these compounds are administered to man.
147 citations
TL;DR: Serumα1-antitrypsin, α1-acid glycoprotein, baptoglobin, ceruloplasmin and C-reactive protein are increased, albumin, transferrin, α-and β-lipoprotein are decreased as an early response to tissue trauma and inflammatory disease and in infection these changes are followed by a rise of γ-globulins.
138 citations
TL;DR: Investigations were done to determine whether this phenomenon occurs in vivo and to delineate the site(s) of acetylation on the albumin molecule to establish a transacetylation reaction between aspirin and human albumin.
Abstract: Acetylsalicylic acid (aspirin) acetylates human serum albumin under physiologic conditions in vitro. These investigations were done to determine whether this phenomenon occurs in vivo and to delineate the site(s) of acetylation on the albumin molecule. Albumin was reacted in vitro with aspirin labeled with (14)carbon at the acetyl-1 or the carboxyl carbon. The altered albumin was hydrolyzed with trypsin and peptide mapping performed. Albumin so treated contains a unique peptide, designated "A," and shows diminution of two normal peptides, designated "B" and "C." Peptide "A" is never seen in normal albumin. Amino acid analyses indicate that peptide "A" equals the sum of peptides "B" and "C." Furthermore all three peptides contain lysine but lack arginine. Thus peptide "A" is formed by the acetylation of a lysine residue which is normally susceptible to trypsin and yields peptides "B" and "C." Radioautography of the peptide maps show most of the acetyl-1-(14)C activity in peptide "A." This indicates that one of the lysine residues in this peptide is the preferential site for the transacetylation reaction. Peptide "A," used as a marker for acetylation, is found in albumin from patients who take aspirin but is not demonstrable in albumin from one of these patients while she was taking sodium salicylate. A transacetylation reaction between aspirin and human albumin occurs in vivo and is similar to that observed in vitro.
137 citations
TL;DR: Bilirubin in micromolar concentrations abolishes respiratory control, uncouples oxidative phosphorylation, and induces swelling of mitochondria, which results in irreversible swelling that is accompanied by proton ejection to the medium.
133 citations
TL;DR: A clonal strain of epithelial cells (designated MH1C1) has been established from the transplantable Morris hepatoma No. 7795 and has maintained distinctive morphology throughout more than 20 subcultures at 2- to 4-week intervals in supplemented Ham's F 10 medium.
Abstract: A clonal strain of epithelial cells (designated MH1C1) has been established from the transplantable Morris hepatoma No. 7795. The cells have maintained distinctive morphology throughout more than 20 subcultures (split 1:5) at 2- to 4-week intervals in supplemented Ham's F 10 medium. They contain many highly refractile, round, cytoplasmic bodies which stain bright red with Oil Red O. The population doubling time was 2 wk when the clonal strain was first established. It has gradually decreased to 1 wk. The cells synthesize rat serum albumin and secrete it into the culture medium as determined immunologically by microcomplement fixation and double diffusion. Albumin secretion (3–6 µg albumin/mg cell nitrogen/24 hr) occurs throughout the logarithmic phase of cell proliferation and has not diminished during serial propagation since the strain was initiated 15 months ago.
128 citations
TL;DR: Excessive loss of protein into the gastrointestinal tract was shown to be a major factor in the hypoproteinemia of patients with giant gastric rugae, regional enteritis, Whipple's disease, gluteninduced enteropathy, ulcerative colitis, intestinal lymphangiectasia and allergic gastroenteropathy.
TL;DR: In patients with cirrhosis of the liver and ascites albumin production was found to be normal or elevated in seven of the 19 subjects, and only markedly depressed in seven patients, in spite of the fact that the serum albumin level was depressed in all patients.
Abstract: The synthesis of serum albumin was measured in 19 patients with cirrhosis of the liver and ascites. Carbonate-(14)C was used to label the guanido carbon of arginine in albumin.18 of the patients had the diagnosis of cirrhosis confirmed by biopsy and/or by the presence of esophageal varices. Seven patients with albumin synthesis rates of 42-105 mg/kg per day demonstrated the lowest serum cholesterol esters and highest serum glutamic oxalacetic transaminase (SGOT) levels, while the seven patients whose albumin synthesis rates ranged from 203-378 mg/kg per day, had significantly higher cholesterol ester levels and significantly lower values for SGOT. The serum albumin levels were equally depressed in all patients. In patients with cirrhosis and ascites albumin production was found to be normal or elevated in seven of the 19 subjects, and only markedly depressed in seven patients, in spite of the fact that the serum albumin level was depressed in all patients.
TL;DR: Reaction of BSA-Q2 with fluorodinitrobenzene suggests that the terminal alpha-amino group, as well as lysine in-AMino groups, are combined with chlorogenoquinone, which is likely to involve the thiol group of bovine serum albumin.
Abstract: 1. The reactions between chlorogenoquinone, the o-quinone formed during the oxidation of chlorogenic acid, and bovine serum albumin depend on the ratio of reactants. 2. When the serum albumin is in excess, oxygen is not absorbed and the products are colourless. This reaction probably involves the thiol group of bovine serum albumin; it does not occur with bovine serum albumin which has been treated with p-chloromercuribenzoate, iodoacetamide or Ellman's reagent. 3. When bovine serum albumin reacts with excess of chlorogenoquinone, oxygen is absorbed and the products are red. The red colour is probably formed by reaction of the lysine in-amino groups of bovine serum albumin, as it is prevented by treating the protein with formaldehyde, succinic anhydride or O-methylisourea. 4. Bovine serum albumin modified by a 1.5-fold (BSA-Q) and a fivefold (BSA-Q2) excess of chlorogenoquinone were separated by chromatography on DEAE-Sephadex A-50, and some of their properties observed. 5. Reaction of BSA-Q2 with fluorodinitrobenzene suggests that the terminal alpha-amino group, as well as lysine in-amino groups, are combined with chlorogenoquinone.
TL;DR: The influence that estrogens and progestins have on the function of the liver in humans and in experimental animals is summarized and modification of current practices does not seem to be indicated.
TL;DR: The determination of the free bilirUBin offers a more precise means of selecting infants at risk to bilirubin encephalopathy.
TL;DR: The results are interpreted as evidence that serum antibody acts as a regulatory mechanism for antibody formation during the conventional antibody response to a metabolizable antigen.
Abstract: Rabbits were injected intravenously with bovine serum albumin (BSA) and bacteriophage T(2) (T(2)). 2-3 wk later, anti-BSA was removed from such animals by a procedure which involved exposure of removed plasma to an immunoadsorbent ((125)I-BSA bound to bromoacetyl cellulose) and return of the adsorbed plasma to the animal. This resulted in removal of the majority of antibody activity to BSA without affecting antibody levels to T(2). 1-2 days later, anti-BSA levels began to rise, and reached peak levels usually 5 days after the removal of antibody. Antibody levels to T(2) did not change. No evidence was obtained that BSA was released from the immunoadsorbent into the circulation of the rabbits. Thus, only trace amounts of radioactivity were released into the plasma; most of the radioactivity was equally coprecipitable with BSA or human gamma globulin and their specific antibodies; the released material was not demonstrated to be immunogenic in primed rabbits; and the released material did not elute with BSA on gel filtration. The results are interpreted as evidence that serum antibody acts as a regulatory mechanism for antibody formation during the conventional antibody response to a metabolizable antigen.
TL;DR: It was found that glutaraldehyde prevented precipitin line formation except at very high titres of antibody in an aldehyde treated bovine serum albumin-rabbit anti-bovine Serum albumin system.
Abstract: The crosslinking effects of formaldehyde, α-hydroxyadipaldehyde and glutaraldehyde have been compared by various techniques. Using a micro-Ouchterlony technique with an aldehyde treated bovine serum albumin-rabbit anti-bovine serum albumin system it was found that glutaraldehyde prevented precipitin line formation except at very high titres of antibody. The effects of formaldehyde and α-hydroxyadipaldehyde were less marked. Cellulose acetate electrophoresis of aldehyde treated bovine serum albumin showed an increase in mobility compared with the untreated protein. Starch gel electrophoresis of aldehyde fixed liver slices showed no protein loss after glutaraldehyde fixation whereas the other aldehydes permitted proteins to be extracted. Polyacrylamide gel electrophoresis of the aldehyde treated bovine serum albumin showed a little change in mobility after formaldehyde and α-hydroxyadipaldehyde treatment and a little polymer formation. Glutaraldehyde on the other hand produced much polymer. These findings were confirmed by gel filtration with Sephadex G-200. Intermolecular crosslinking with glutaraldehyde was dependant on the aldehyde concentration.
TL;DR: The phospholipid enhancement of cholesterol excretion was demonstrated in L5178Y cells prelabeling with exogenous cholesterol and L-cells prelabeled with biosynthesized cholesterol.
TL;DR: The interaction of the anticoagulant drug warfarin and its metabolites with human plasma albumin was studied by equilibrium dialysis and suggests cooperative hydrogen and hydrophobic bonding as the molecular basis for the binding of warFarin to albumin.
Abstract: The interaction of the anticoagulant drug warfarin and its metabolites with human plasma albumin was studied by equilibrium dialysis. A 20-fold variation of buffer ionic strength (0.017-0.340) caused no significant change in the warfarin association constant. But the binding strength rose significantly as the pH was increased from 6.0 to 9.0 and then declined at pH 10.0. The 6-, 7-, and 8-hydroxywarfarin metabolites showed a 7- to 23-fold reduction in binding strength at pH 10.0. These data indicate that the molecular basis of the interaction is nonelectrostatic and that the introduction of polar hydroxyl groups on the coumarin nucleus by metabolism reduces its hydrophobic binding surface. The interaction was markedly exothermic and showed a positive entropy (increased molecular disorder), which suggests cooperative hydrogen and hydrophobic bonding as the molecular basis for the binding of warfarin to albumin. The marked albumin binding and nonpolar character of warfarin explains the respective absence and presence of the unchanged drug in urine and plasma of warfarintreated patients, while the more polar character and lesser albumin binding of the metabolites probably determines their absence in plasma and presence in urine. The relatively marked binding to albumin of the 4'-hydroxywarfarin metabolite suggests that it may occur in the plasma of warfarin-treated patients. The data suggest that a direct correlation exists between the interaction of warfarin with plasma albumin and the interaction with the warfarin receptor site.
TL;DR: An enzyme which catalyzes the transfer of arginine from tRNA to protein has been partially purified from the soluble fraction of rabbit liver cytoplasm and a tetrapeptide containing 80% of the radioactiveArginine incorporated into albumin has been obtained.
TL;DR: Evidence is presented supporting the concept that a greatly disordered conformation is an intermediate and the fluorescence life-times of pyrenebutyric-bovine serum albumin conjugates appears to be a linear function of quantum yield.
TL;DR: At acid pH, bovine serum albumin enhances the rate at which glucose diffuses from lecithin-cholesterol-dicetyl phosphate micelles, which is close to the pH at which the well-known acid conformation change occurs in this protein.
TL;DR: The crosslinking abilities of osmium tetroxide, potassium dichromate and potassium permanganate towards bovine serum albumin and bovines γ-globulin were investigated by chromatography with Sephadex G-200 and the oxidative cleavage of the proteins by these oxidative fixation agents was studied.
Abstract: The crosslinking abilities of osmium tetroxide, potassium dichromate and potassium permanganate towards bovine serum albumin and bovine γ-globulin were investigated by chromatography with Sephadex G-200. Osmium tetroxide had a moderate crosslinking ability towards these proteins, the others had little or none. Chromatography with Sephadex G-50 permitted the oxidative cleavage of the proteins by these oxidative fixation agents to be studied. Potassium permanganate caused much fragmentation of the proteins and destruction of the tyrosine and tryptophan residues. Osmium tetroxide and potassium dichromate caused only a small amount of protein cleavage. These results were corroborated by polyacrylamide gel electrophoresis and viscosimetric studies. The significance of the results for tissue fixation is discussed.
TL;DR: The data regarding magnesium in alcoholism indicate a a high frequency of low serum magnesium levels, particularly in delirium tremens, which is poorly correlated with the other physiologic abnormalities measured.
Abstract: The ‘illness that causes an alcoholic patient to seek medical assistance arises from complex disturbances in physiology, representing a combination and interplay of various deficiencies and imbalances in body constituents. Among these, depression of the serum magnesium constant has received much However, lowered serum magnesium, though frequently found in these patients, is difficult to interpret, both in relation to symptoms and as an indicator of total body deficiency or maldistribution of magnesium. Inadequate magnesium intake, protein calorie malnutrition, increased loss through vomiting, and urinary loss associated with ethanol metabolism, are factors conductive to magnesium deficiency in the alcoholic. Each of these presents equally difficult problems in evaluation. The purpose of this study is to measure and analyze recognized physiologic variants occurring in alcoholism, particularly in the alcoholic withdrawal syndrome and its most serious manifestation, delirium tremens. The role or significance of abnormalties in serum magnesium will be examined in reference to the entire complex of physiologic disturbances. We shall find of particular interest the incidence of low serum magnesium in the alcoholic patient, its relation to symptoms, to red cell magnesium content, to thiamine deficiency, to hepatic dysfunction, and to hypertriglyceridemia; its association with alterations of serum sodium, potassium, or calcium; and the relation of urinary excretion of magnesium to serum magnesium levels and to associated cation and anion urinary loss. One of the major problems in this field is q e validity of low serum levels as indicators of generalized magnesium deficiency. Disturbances in calcium and phosphorus metabolism have been described in experimental magnesium def i~ i ency .~ Evidence of these disturbances was sought in our alcoholic patients. The data regarding magnesium in alcoholism, derived from this study, indicate a a high frequency of low serum magnesium levels, particularly in delirium tremens. This depression of serum magnesium is poorly correlated with the other physiologic abnormalities measured. It appears to be infrequently associated with decreased red cell magnesium, decreased muscle magnesium, or other evidence of total body magnesium deficit. Failure of the kidney to retain magnesium appears to be a major contributing factor, although its mechanism remains uncertain.
TL;DR: It is found that incubation of adipose tissue slices from rabbit, hamster or rat in the homologous serum containing 10 μg/mlACTH or epinephrine causes, in association with the hormone-stimulated lipolysis, a 40–49 % decrease in medium calcium and a 150–460% increase in tissue calcium.
Abstract: Injection of 50 U adrenocorticotropin (ACTH) in rabbits produces 3 hr later a 260–680 % increase in serum FFA concentration, a 27% reduction in the concentration of calcium in serum, and a 500–1100% increase in the concentration of calcium in adipose tissue. Incubation of adipose tissue slices from rabbit, hamster or rat in the homologous serum containing 10 μg/mlACTH or epinephrine causes, in association with the hormone-stimulated lipolysis, a 40–49 % decrease in medium calcium and a 150–460% increase in tissue calcium. When the incubation medium is Krebs-Ringer buffer +bovine serum albumin instead of serum, a similar degree of lipolysis is stimulated in rabbit adipose tissue by ACTH, but no detectable redistribution of calcium from medium to tissue occurs. (Endocrinology 84: 926, 1969)
TL;DR: The results did not exclude the possibility that the tear albumin was a modified form of the albumin or prealbumin found in serum, as was the case with secretory IgA, which consists of serum IgA attached to a “transport piece”4.
Abstract: A MAJOR, poorly characterized component of human tears migrates more anodally than serum albumin in electrophoresis1. Erickson termed this protein “tear albumin”. When they carried out immunoelectrophoresis of human tears with rabbit anti-human tear serum, Josephson and Lockwood2,3 obtained a precipitin line in the albumin region. This line did not disappear when the anti-tear serum was absorbed with normal human serum. These results1–3 did not exclude the possibility that the tear albumin was a modified form of the albumin or prealbumin found in serum, as was the case with secretory IgA, which consists of serum IgA attached to a “transport piece”4.
TL;DR: P pH-solubility fractionation of the monomer showed that it contained about 80% of material with the same optical rotation, pH- solubility properties, tryptophan fluorescence, and binding properties as native serum albumin, indicating that the formation of the tertiary structure of BSA during its biosynthesis is influenced by lipids which are bound to it.
TL;DR: The blood serum of the eastern diamond back rattlesnake neutralizes lethal doses of C. adamanteus venom in mice and forms precipitin bands on immunophoresis against venom.
Abstract: The blood serum of the eastern diamond back rattlesnake (Crotalus adamanteus) neutralizes lethal doses of C. adamanteus venom in mice. The protective capacity of the serum is associated with the serum albumin, rather than the immunoglobulin fraction of the blood. Neither the serum nor its albumin fraction form precipitin bands on immunophoresis against venom.