Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00631 (Gel)
 14,881 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A method for covalent coupling of bilirubin to albumin is described. Human serum albumin-bilirubin (1:1 complex) has been treated with water soluble carbodiimide in order to obtain covalent coupling of bilirubin to albumin. The reaction conditions have been varied with respect to pH, reaction time and concentration of reagent to obtain the optimal coupling. The prepared albumin-bilirubin compounds were investigated by spectrophotometry, gel filtration and gel electrophoresis to ascertain the covalent nature of the bond and to characterize the products further. Gel electrophoresis and gel filtration showed that a monomer fraction could be prepared, and this fraction was a suitable material for further studies.
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PMID:Covalent coupling of bilirubin to albumin. 0 97

We used a modification of the TSH radioreceptor assay to detect TSH-binding inhibition (TBI) activity in serum and serum fractions from normal subjects and patients with Graves' disease. TBI activity is present in normal IgG prepared by DEAE-Sephadex chromatography and in normal globulins prepared by precipitation at 1.6 M ammonium sulfate. Other normal serum proteins also had TBI activity when large concentrations were tested. Gel filtration chromatography and powder block electrophoresis were used to prepare fractions of normal and Graves' disease sera. In these fractions from normal serum. TBI activity was found in both gamma-globulin and alpha-globulin-albumin fractions electrophoretically and in both 7S and 4S peaks from gel filtration. TBI activity from Graves' disease patients' sera was similarly distributed, but relatively more TBI accompanied the electrophoretic gamma-globulins. Sepharose Protein-A and anti-IgG were used as immunoabsorbents to isolate and purify IgG from normal and Graves' disease sera. TBI activity in IgG was proportional to the IgG concentration, indicating that the TBI which migrates as a gamma-globulin electrophoretically is an IgG and thus may possibly be an antibody. Inhibitory activity found in normal serum globulins and the non-IgG fractions of both normal and abnormal sera seriously interferes with attempts to use the TSH radioreceptor assay to study the hypothesized anti-TSH, receptor antibody in the serum of patients with Graves' disease.
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PMID:Serum protein inhibition of thyrotropin binding to human thyroid tissue. 4 74

Intact, washed Trypanosoma lewisi bloodstream forms, isolated from rats, were agglutinated specifically by antisera against rat whole serum, albumin, alpha2-macroglobulin, and IgG. However, trypsinized bloodstream and intact culture forms lacking surface coat were not agglutinated by these antisera. Trypsinized bloodstream forms, incubated in dilute rat or heterologous host serum proteins, were agglutinated with specific antisera. The characteristic surface coat of intact bloodstream forms was absent from trypsinized cells; however, trypsinized and serum-incubated bloodstream forms reacquired a surface coat similar to that of intact cells. Gel-diffusion and immunoelectrophoretic results showed that rat albumin, alpha2-macroglobulin, and IgG were present in the surface coat of bloodstream forms. Results of quantitative rocket immunoelectrophoresis demonstrated that the adsorbed rat serum proteins constituted by weight about 5% of the trypanosome total surface coat protein.
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PMID:Immunologic and fine structure evidence of avidly bound host serum proteins in the surface coat of a bloodstream trypanosome. 5 18

Gel filtration of human platelet-rich plasma (PRP) on columns of Sepharose 2B removed at least 99.85% of the plasma proteins from platelets when a column 10 cm in height was used and a plasma volume 11 to 14% of the gel-bed volume was applied. ADP and ATP levels in gel-filtered platelets (GFP) were not significantly different from those in PRP. By transmission electron microscopy, GFP were indistinguishable from PRP. Gel filtration appears to be a highly satisfactory technique of separating platelets from plasma without modifying structure, function, or contents significantly. The roles of several crude protein fractions in platelet aggregation and aspirin's inhibition of aggregation were examined. Fraction I (mostly fibrinogen) enhanced collagen-induced aggregation of gel-filtered platelets; Fraction V (mostly albumin) was inhibitory. Fraction II (mostly gamma-globulin) or gelatin had no significant effect. Aspirin added to gel-filtered platelets inhibited aggregation by 80%. The addition of mixtures of plasma proteins containing albumin increased albumin's inhibitory effect. Incubation of gel-filtered platelets with aspirin labeled in the carboxyl position resulted in no uptake of the label. In contrast, incubation with acetyl-labeled aspirin was followed by uptake of more than 2 X 10(6) acetyl groups per platelet in 1 minute. Incubation for 30 minutes resulted in a five- to sixfold further increase in uptake of the label. Aspirin can acetylate platelets and inhibit aggregation directly. Plasma proteins, in particular albumin or a contaminant of the albumin fraction tested, enhance the inhibitory effect of aspirin on platelet aggregation.
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PMID:Gel-filtered human platelets. Ultrastructure, function, and role of proteins in inhibition of aggregation by aspirin. 5 50

One and 24 hours after the administration of 63NiCl2 and 63Ni(CO)4 to mice 63Ni was present in association with both particulate and soluble cellular constituents in the lung, liver and kidney. After disruption of the cellular organells by sonication, a considerable part of the 63Ni was still bound to the cellular fragments. Sephadex G-75 chromatography of the cytosol of the lung showed that the largest proportion of 63Ni was eluted in the void volume and a smaller proportion was present in the salt volume. In the kidney, the proportions were reversed. Twentyfour hours after the injection of 63NiCl2 an intermediate 63Ni-containing peak, with an estimated molecular weight of about 30,000, was found in the lung and the kidney. In the liver of 63 NiCl2-injected mice, most of the nickel was recovered in the void volume, a lesser amount in the salt volume. There was no evidence that 63Ni was bound to metallothionein (induced by Cd-pretreatment) or to superoxide dismutase in the studied tissues. Pretreatments with non-labelled NiCl2 did not alter the elution profiles. In serum, most 63Ni was present in association with albumin. Gel-chromatograms of red blood-cell hemolysates from 63Ni(CO)4-injected mice showed 63Ni at an elution volume corresponding to hemoglobin, but 63Ni-binding ligands with higher and lower molecular weights were also present.
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PMID:Binding of 63Ni by cellular constituents in some tissues of mice after the administration of 63NiCl2 and 63Ni(CO)4. 11 36

We have perfused isolated rat livers with hypocalcemic (4.4 mg 100 ml) Krebs-Ringer bicarbonate albumin buffer. After 15 min of perfusion, a substance appeared in the perfusate which decreased rat renal adenylate cyclase activation by parathyroid hormone (PTH). The material in the perfusate was purified greater than 50,000-fold by Bio-Gel P-10 chromatography. The purified antagonist decreased the activation of rat renal cortical adenylate cyclase by PTH, glucagon, and epinephrine 75 to 100%. Concentration response curves for each of the hormones indicated a noncompetitive interaction of the inhibitor with the hormone. The inhibition was not species-specific, as the activation of the parathyroid hormone-responsive adenylate cyclase in cat renal cortex was also abolished by the inhibitor from the perfused rat liver. The inhibitor is a peptide, Mr equal to similar to 1000, which is heat-stable, acid-stable, alkai-labile, and is destroyed by trypsin, leucine aminopeptidase, and elastase. It is not destroyed by phosphodiesterase, 5'-nucleotidase, alkaline phosphatase, neuraminidase, RNase, or phospholipase A. The inhibitor is not produced by isolated rat livers perfused with normocalcemic perfusion media. It is unclear whether the peptide is synthesized by the liver or whether it is a breakdown product of a larger peptide or protein in the liver. This is the first reported peptide inhibitor of adenylate cyclase.
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PMID:Isolation of a unique peptide inhibitor of hormone-responsive adenylate cyclase. 16 24

Immunoreactive glucagon (IRG) fractions from plasma of 8 normal subjects and 4 patients with glucagon secreting tumors were studied by gel filtration techniques on Bio Gel P--30 and Sephadex G--50 columns. The pancreatic glucagon specific anti serum (30K) of Unger was utilized to measure IRG. Columns were calibrated with labelled albumin, proinsulin, insulin and glucagon. Four peaks were defined in normal and tumor bearing patients: peak I (greater than 20 000 mol. wt.), peak II (primarily 9000 mol. wt.), peak III pancreatic glucagon (3500 mol. wt.) and peak IV small gucagon (less than 3500 mol. wt.). Glucagonoma patients differed from our normal and reported normal subjects in that peak II contained most of the circulating IRG. The percent of IRG associated with peak II was 9.5--31.5% in normals and 39.1--61.2% in glucagonomas. Glucagon-like biological activity in an isolated hepatocyte system was demonstrated for all peaks. However, relative to immunoreactivity, peak II showed reduced activity (25--33%). Immunoassay of dilutions of all peaks revealed the probability of immuno determinants identical with procine pancreatic glucagon. The presence of heterogenous IRG peaks with biological glucagon-like activity suggest that the larger molecules may be prohormones. Further, it is possible that specific elevation of peak II may be a diagnostic feature of glucagonomas.
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PMID:Plasma immunoreactive glucagon fractions in four cases of glucagonoma: increased "large glucagon-immunoreactivity". 18 97

Entamoeba histolytica (HK-9: IMSS) trophozoites were separated from the culture medium and washed and submitted to the effects of ultrasound during 10 minutes. After 10,000 rpm x 30 centrifugation, the supernatant fluid was separated in four fractions by Sephadex G-200 gel chromatography. These fractions were lyophilized, redisolved in a lesser volume and dyalized against isotonic saline solution. Antigen-antibody precipitant reactions between each of them and two rabbit antiserums were demonstrated: anti amoeba and anti fraction A. It was verified that the antisera reacted also with the culture medium, the human seric albumin and the sera from health people and patients with invasive amebiasis. The higher antigenicity, quantitatively and qualitatively, was obtained with the fraction B; the less antigenic fraction was the fraction D. In fraction A three antigens were identified. When those proteins were filtered by a Bio Gel P4 column, two fractions were eluted: A1 and A2 which were lyophilized, redisolved and dyalized in isotonic saline solution. After this treatment, fraction A1 was capable to maintain its antigenicity against the rabbit antisera and the sera from patients with invasive amebiasis, fact by which it was considered a protein from amebal origin and not as a protenic contaminant from the culture medium.
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PMID:[Immunochemistry of immunogenic proteins of Entamoeba histolytica]. 21 45

Gel filtration of fresh human serum revealed that over 95% of the thymic-hormone-like activity was present in the fraction representing the total albumin and prealbumin. Further studies demonstrated that the activity resided in the prealbumin fraction; albumin was inactive. Prealbumin was isolated from Cohn fraction IV-1 of pooled human plasma by extraction with aqueous buffer, fractionation with (NH4)2SO4, gel filtration on Sephadex G-150, and preparative disc gel electrophoresis. The final product was homogeneous by analytical gel electrophoresis was 40,000 times more active than the starting material in an azathioprine-sensitive rosette assay. Physical and chemical characterization studies showed that the isolated product was identical to authentic human plasma prealbumin. Isolation of the prealbumin fraction from sera of adult thymectomized mice revealed that the rosette activity was substantially lower than that isolated from sera of normal mice, suggesting a thymic dependence of the prealbumin activity. In vitro and in vivo bioassays of the fraction obtained prior to the final step of the purification procedure support the conclusion that prealbumin exhibits thymic hormone-like activity.
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PMID:Thymic hormone-like restoration by human prealbumin of azathioprine sensitivity of spleen cells from thymectomized mice. 27 45

An antigen-dependent factor showing migration inhibition (MIF) and gold uptake stimulation (GUS) activities which has been previously described (Lowe & Lachmann, 1974) has been further purified from efferent lymph collected from cannulated nodes of BCG-sensitized sheep undergoing a delayed hypersensitivity response to PPD. During purification, fractions containing MIF activity also exhibited GUS activity. Initial purification by salt precipitation showed that antigen-dependent MIF activity was in the 40-90% ammonium sulphate precipitate. Non-specific activity and contaminating immunoglobulin were found in the 0--20% and 20--40% precipitates. Gel filtration on Sephadex G-200 and affinity chromatography on Concanvalin A-Sepharose have shown that antigen-dependent MIF is a glycoprotein of approximately 70,000 molecular weight (Lowe & Lachmann, 1974). Traces of contaminating antibody in the glycoprotein fraction were removed by immuno-adsorption on monospecific anti-sheep IgG-Sepharose. Antigen-dependent MIF was also purified by affinity chromatography on PPD-Sepharose. The eluted fractions with all the antigen-specific activity, contained less than 1% of the applied material. Analysis by polyacrylamide gel electrophoresis showed that the major protein component in the purified MIF preparation has a molecular weight and electrophoretic mobility identical with that of sheep albumin. Although this represents a high degree of purification of antigen-dependent MIF it seems that albumin is still present as a contaminant and that the protein associated with MIF activity is present in trace quantities.
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PMID:Purification of antigen-dependent macrophage migration inhibition factor (MIF) from lymph draining a tuberculin reaction. 36 99


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