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Emergence of beta-adrenergic sensitivity in the developing chicken heart.

Lipshultz, S; Shanfeld, J; Chacko, S
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1981 EN
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Muscle cells dissociated from 5-day embryonic chicken hearts showed dose-dependent increases in both chronotropic rates of contraction and cyclic AMP (cAMP) levels in response to epinephrine (EPI), an effect that could be blocked by beta-adrenergic antagonists. However, 2- to 2.5-day embryonic chicken myocardial cells, although similar to 5-day heart cells with respect to the organization of myofibrils, failed to respond to EPI either by increased rates of contraction or by elevated levels of intracellular cAMP. Development of beta-adrenergic sensitivity in 2- to 2.5-day cells did not occur even after several days of growth in culture. However, addition of an extract prepared from 11-day chicken embryos to 2- to 2.5-day muscle cell cultures at any point during in vitro growth resulted in the development of sensitivity to EPI as measured by increases in both the beating frequency and cAMP levels after a 48-hr incubation in embryo extract (EE). The basal level of cAMP in cells unresponsive to EPI is 5 times that in EPI-sensitive muscle cells from older hearts (5 days). The high basal level of cAMP in these cells is reduced to a level characteristic of cells from older hearts when treated with the EE. Once sensitivity was acquired, it was retained as a stable trait of the muscle cells in culture. Furthermore...

High molecular weight peptide with corticotropin-releasing factor activity from porcine hypothalami.

Schally, A V; Chang, R C; Arimura, A; Redding, T W; Fishback, J B; Vigh, S
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /08/1981 EN
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The presence of a corticotropin-releasing factor (CRF) behaving as a peptide with a molecular weight of about 5000 was established after purification of porcine hypothalamic extracts by gel filtration on Sephadex G-25 and then on Sephadex G-50. Purified CRF stimulated the release of corticotropin (ACTH) in three in vitro systems: isolated rat pituitary quarters, monolayer cultures of dispersed pituitary cells, and superfused pituitary cells on a column. A linear logarithmic dose-response relationship existed between 50 and 200 micrograms of CRF preparations per ml and the total amount of ACTH released by the superfused pituitary cells. The pituitary ACTH response to CRF in the pituitary quarters system was also approximately linearly related to the logarithm of the dose of CRF. CRF also stimulated in vivo release of ACTH in rats pretreated with chlorpromazine, morphine, and Nembutal. CRF activity was labile to digestion with trypsin and chymotrypsin and was partially destroyed by pepsin. The evidence indicates that CRF of porcine origin is a polypeptide of a higher molecular weight than previously assumed.

A new method for isolating the nonidentical protein subunits of human plasma α-lipoprotein

Rudman, Daniel; Garcia, Luis A.; Howard, Carolyn H.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /02/1970 EN
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Human plasma alpha lipoprotein (αLP) was totally delipidated by gel filtration on Sephadex LH-20 in a medium of 2 butanol:acetic acid:H2O, 4:1:5. The resulting alpha protein (αP) exhibited two major bands, labeled C and D, on acrylamide-gel electrophoresis in 5.0 M urea at pH 8.8 or 4.0. Minor bands labeled A and B, also present, were shown to be aggregates of C which form when the latter is lyophilized. The C and D components were isolated in pure form from αP (prepared by LH-20 chromatography of αLP) by gel filtration of this protein on Sephadex G-200 in a medium of 1.0 N acetic acid: the C component emerged with a distribution coefficient (Kd) of 0.4, and the D component with a coefficient of 0.7. From each 100 mg of αP, 68 mg of C and 22 mg of D were isolated. 3 mg of a minor fraction with Kd 0.1, containing A and B components as well as C, were also obtained. D but not C reacts with rabbit antiserum to human αLP. C and D differ substantially in content of arginine, histidine, ½-cystine, isoleucine, and tryptophan.

Hormone synthesis and secretion by rat parathyroid glands in tissue culture

Au, William Y. W.; Poland, Alan P.; Stern, Paula H.; Raisz, Lawrence G.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /09/1970 EN
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Rat parathyroid glands maintained in organ culture secrete biologically active parathyroid hormone (PTH) and synthesize and secrete labeled proteins from 3H- or 14C-labeled amino acids added to the medium. The amounts of biological activity and labeled protein in the medium are both inversely proportional to the calcium concentration. Some of the labeled low molecular weight protein was identified as PTH which had been synthesized and secreted in culture by preliminary isolation on Sephadex G-100 columns and further purification using an antibody to bovine PTH which cross-reacted with rat PTH. The cross-reacting antibody inhibited the biological effects of rat PTH and caused hypocalcemia in intact rats. The antibody bound some of the labeled low molecular weight protein of the medium at neutral pH so that it migrated as a large molecular weight complex on Sephadex. Biologically active, labeled PTH was recovered by dissociation of this complex in acid and rechromatography.

Biosynthesis of Vasopressin In Vitro and Ultrastructure of a Bronchogenic Carcinoma: PATIENT WITH THE SYNDROME OF INAPPROPRIATE SECRETION OF ANTIDIURETIC HORMONE

George, Jack M.; Capen, Charles C.; Phillips, Audra S.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1972 EN
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Tumors from patients with the syndrome of inappropriate secretion of antidiuretic hormone (SIADH) have been found to contain large amounts of the antidiuretic hormone vasopressin. A lung tumor from a patient with hyponatremia most likely due to SIADH was removed at surgery and found to contain 23.5 mU vasopressin/g wet weight by radioimmunoassay Slices of this tumor were incubated with phenylalanine-3H. Arginine vasopressin-3H was purified from the incubate by Sephadex G-25 column chromatography in two different systems, performic acid oxidation, and gradient elution column chromatography with diethylaminoethyl Sephadex. As oxidation of vasopressin results in drastic conformational change with breaking of the ring of the cyclic polypeptide and addition of two cysteic acid residues per molecule, the radioactive material which eluted coincident with vasopressin both before and after this procedure was considered to be arginine vasopressin-3H. To our knowledge this is the first demonstration of in vitro biosynthesis of vasopressin by a tumor from a patient with SIADH.

Regulation of 6-phosphofructo-2-kinase activity by cyclic AMP-dependent phosphorylation.

el-Maghrabi, M R; Claus, T H; Pilkis, J; Pilkis, S J
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1982 EN
Relevância na Pesquisa
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Addition of glucagon to isolated rat hepatocytes resulted in inhibition of 6-phosphofructo-2-kinase (ATP:D-fructose-6-phosphate-2-phosphotransferase) activity in extracts of the cells and in a decrease in the intracellular level of fructose 2,6-bisphosphate. The effect on 6-phosphofructo-2-kinase was characterized by a decrease in the affinity of the enzyme for fructose 6-phosphate. To investigate the mechanism of action of glucagon, 6-phosphofructo-2-kinase from rat liver was partially purified by polyethylene glycol precipitation, DEAE-cellulose chromatography, (NH4)2SO4 fractionation, Sephacryl S-200 gel filtration, DEAE-Sephadex chromatography, and Sephadex G-100 gel filtration. Incubation of the purified enzyme with the catalytic subunit of the cyclic AMP-dependent protein kinase from rat liver and [gamma-32P]ATP resulted in 32P incorporation into a protein with a subunit Mr of 49,000 as determined by NaDodSO4 disc gel electrophoresis. Associated with this phosphorylation was an inhibition of 6-phosphofructo-2-kinase activity that was also characterized by a decrease in the affinity of the enzyme for fructose-6-phosphate. Both the phosphorylation and the inhibition of the purified 6-phosphofructo-2-kinase were blocked by addition of the heat-stable protein kinase inhibitor. It is concluded that the glucagon-induced decrease in fructose 2...

Purification and immunochemical characterization of Streptococcus sanguis serotype I carbohydrate antigen.

Okahashi, N; Koga, T; Akada, H; Hamada, S
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /02/1983 EN
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The serotype-specific antigen of Streptococcus sanguis ST3 (serotype I, biotype A) was extracted, chromatographically purified, and characterized by immunological and chemical methods. The antigen was extracted from purified cell walls with hot trichloroacetic acid, followed by ion-exchange chromatography on a DEAE-Sephadex A-25 column and gel filtration through a Sephadex G-100 column. A peak fraction was obtained that gave a single precipitin band when reacted with anti-type I serum. The type I antigen was a polysaccharide composed of glucose, rhamnose, and N-acetylglucosamine in a molar ratio of 1.4:2.5:1.0. Quantitative precipitin inhibition tests with various haptenic sugars indicated that an alpha-glucosidic linkage is the immunodeterminant of the type I antigen.

Purification and some properties of a non-o1 Vibrio cholerae enterotoxin that is identical to cholera enterotoxin.

Yamamoto, K; Takeda, Y; Miwatani, T; Craig, J P
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1983 EN
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Cholera-like enterotoxin was isolated and purified from the culture supernatant of a non-O1 strain of Vibrio cholerae, E8498, isolated from the environment. Enterotoxin was purified by aluminum hydroxide absorption and elution and successive gel filtrations on Sephadex G-100, Bio-Gel A-5m, and Sephadex G-75. Purified enterotoxin gave a single stained band on polyacrylamide gel disc electrophoresis, and the mobility was the same as that of cholera enterotoxin. The specific biological activity of the purified enterotoxin was almost the same as that of cholera enterotoxin in the Chinese hamster ovary cell assay, fluid accumulation in mouse ligated intestine, increase in vascular permeability in rabbit skin, and passive immune hemolysis. Sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis showed that the purified enterotoxin consisted of subunits A and B, identical to those of cholera enterotoxin, and Ouchterlony double gel diffusion tests indicated that the two toxins were immunologically identical. Enterotoxins prepared from several non-O1 strains isolated from human patients were also immunologically identical to cholera enterotoxin.

Arachidonate metabolism via lipoxygenase and 12L-hydroperoxy-5,8,10,14-icosatetraenoic acid peroxidase sensitive to anti-inflammatory drugs.

Siegel, M I; McConnell, R T; Porter, N A; Cuatrecasas, P
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1980 EN
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The enzymes of arachidonate metabolism via the lipoxygenase pathway in human platelet cytosol have been characterized and partially purified. The lipoxygenase activity has a pH optimum of 7.3 and reaches half-maximal activity at an arachidonate concentration of 80 microM. The oxidation of arachidonate by these enzymes is inhibited by reagents that modify sulfhydryl groups. Two separable lipoxygenase activities can be detected by chromatography of platelet cytosol on Sephadex G-150 and of partially purified preparations on DEAE-Sephadex. One of these has an apparent Mr of 100,000. A second enzyme species behaves as a Mr 160,000 entity containing, in addition to lipoxygenase, a peroxidase activity that catalyzes the conversion of 12L-hydroperoxy-5,8,10,14-icosatetraenoic acid (HPETE) to 12L-hydroxy-5,8,10,14-icosatetraenoic acid (HETE). Aspirin, indomethacin, sodium salicylate, phenylbutazone, ibuprofen, naproxen, and sulindac, but not acetaminophen or phenacetin, give rise to increased levels of HPETE in the lipoxygenase pathway. This increase in HPETE levels is the result of the ability of these drugs to inhibit directly the enzymatic conversion of HPETE to HETE.

Selenium-containing tRNAs from Clostridium sticklandii: cochromatography of one species with L-prolyl-tRNA.

Chen, C S; Stadtman, T C
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1980 EN
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75Se-Labeled tRNAs were synthesized by Clostridium sticklandii cultures supplemented with 1 microM sodium [75Se]selenite or [75Se]selenocysteine. This process is highly specific for selenium; it occurred in the presence of 1.2 mM sodium sulfide and was not decreased by the further addition of a 500-fold molar excess of cysteine. The 75Se in these tRNAs was located in the polynucleotide portion of the molecules and not in esterified (alkali-labile) selenocysteine. Inhibition of cell multiplication by antibiotics that block either protein synthesis or DNA-dependent RNA synthesis did not prevent this 75Se incorporation. Three [75Se]tRNAs were separated from C. sticklandii cells labeled in the presence of chloramphenicol and were partially purified by chromatography on benzoylated DEAE-cellulose and DEAE-Sephadex A-50 columns. These were designated seleno-tRNAs I, II, and III according to their elution sequence from benzoylated DEAE-cellulose. Cochromatography of purified seleno-tRNA II on DEAE-Sephadex A-50 with an L-proline-accepting species suggests that it is a selenium-containing L-prolyl-tRNA.

Immunologic effects of whole-body ultraviolet irradiation: selective defect in splenic adherent cell function in vitro.

Letvin, N L; Greene, M I; Benacerraf, B; Germain, R N
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /05/1980 EN
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Splenocytes from mice receiving whole-body UV irradiation do not make a normal primary in vitro plaque-forming cell (PFC) response to the soluble T-dependent antigen trinitrophenylated poly(L-glutamic acid60L-alanine30L-tyrosine10). This impaired immune response results from a selective loss of antigen-presenting cell function in the splenic adherent cell (SAC) population of the UV-treated mice. SACs from UV-irradiated mice are unable to reconstitute a PFC response when added to normal splenocytes passed through Sephadex G-10 (which depletes adherent cells), whereas normal SACs, when added to Sephadex G-10-passed splenocytes from UV-treated mice, do restore a PFC response. The effect of in vivo UV irradiation on the SAC population is indistinguishable functionally from the effect of in vitro UV irradiation of SACs from normal mice. Possible explanations for this selective effect of external UV irradiation on SAC function are discussed.

Further purification and characterization of heat-stable enterotoxin produced by Yersinia enterocolitica.

Okamoto, K; Inoue, T; Shimizu, K; Hara, S; Miyama, A
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1982 EN
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Heat-stable enterotoxin (ST) of Yersinia enterocolitica was produced under defined conditions. It was first detected in the culture supernatant of the late-logarithmic phase of growth and increased lineally during the the stationary phase of growth. The ST level became maximum at the decline phase of growth, and the ST was not detected in the lysate of bacteria obtained from the decline phase of growth. The ST was extensively purified from the culture supernatant, and about a 1,905-fold purification was achieved with a yield of 8.9%. The minimal effective dose of the purified ST was approximately 25 ng in the suckling mouse assay. The purified ST gave a single 280-nm absorbing peak on polyacrylamide disc gel electrophoresis and had a maximum absorption at 272 nm, and its molecular weight was 9,700 by Sephadex G-75 superfine gel filtration. The biological activity of the purified ST was lost by treatment with 2-mercaptoethanol, suggesting that the ST contained disulfide bridges in the molecule which were required for the development of toxic activity. The purified ST was heat stable at 100 degrees C for 10 min between pH 2.2 and 8.0, but not at pH values greater than 9.0 or in 2 N HCl. The treatment of the ST with trypsin resulted in a retarded elution of the ST activity by Sephadex F-75 superfine gel filtration and a passage through a UM-20 membrane filter.

Purification of a Streptococcal Bacteriocin (Viridin B) and Its Separation from Alpha-Hemolysin

Apelgren, Lynn D.; Dajani, Adnan S.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1979 EN
Relevância na Pesquisa
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Viridin B, a bacteriocin produced by Streptococcus mitis, copurified with the alpha-hemolysin after ammonium sulfate precipitation and gel filtration on Sephadex G-200. The bacteriocin and hemolysin were separated in some instances by ion-exchange chromatography on diethylaminoethyl-Sephadex A-50, but the two substances were shown to be distinct after polyacrylamide gel electrophoresis. Attempts at recovery of nonhemolytic or nonbacteriocinogenic mutants were unsuccessful after exposure to mutagenic agents. The molecular weight of viridin B was determined to be approximately 87,000.

Purification and characterization of the DNA polymerase and RNase H activities in Moloney murine sarcoma-leukemia virus.

Gerard, G F; Grandgenett, D P
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /04/1975 EN
Relevância na Pesquisa
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Two RNase H (RNA-DNA hybrid ribonucleotidohydrolase, EC 3.1.4.34) activities separable by Sephadex G-100 gel filtration were identified in lysates of Moloney murine sarcoma-leukemia virus (MSV). The larger enzyme, which we have called RNase H-I, represented about 10% of the RNase H activity in the virion. RNase H-I (i) copurified with RNA-directed DNA polymerase from the virus, (ii) had a sedimentation coefficient of 4.4S (corresponds to an apparent mol wt of 70,000), (iii) required Mn-2+ (2 mM optimum) for activity with a [3-h]poly(A)-poly(dT) substrate, (iv) eluted from phosphocellulose at 0.2 M KC1, and (v) degraded [3-H]poly(A)-poly(dT) and [3-H]poly(C)-poly(dG) at approximately equal rates. The smaller enzyme, designated RNase H-II, which represented the majority of the RNase H activity in the virus preparation, was shown to be different since it (i) had no detectable, associated DNA polymerase activity, (ii) had a sedmimentation coefficient of 2.6S (corresponds to an apparent mol wt of 30,000), (iii) preferred Mg-2+ (10 to 15 mM optimum) over Mn-2+ (5 to 10 mM optimum) 2.5-fold for the degradation of [3-H]poly(A)-poly(dT), and (iv) degraded [3-H]poly(A)-poly(dT) 6 and 60 times faster than [3-H]poly(C)-poly(dG) in the presence of Mn-2+ and Mg-2+...

Methylation pattern of genomic RNA from Moloney murine leukemia virus.

Bondurant, M; Hashimoto, S; Green, M
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /09/1976 EN
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32P- and methyl-3H-labeled 70S Moloney murine leukemia virus RNA was purified from virions produced in Moloney murine leukemia virus-infected mouse embryo cells. Primer-free RNA subunits obtained by heat treatment and zonal centrifugation were digested with RNase T2, and methylated oligonucleotides were chromatographed on DEAE-Sephadex in 7 M urea. Approximately one molecule of RNase T2-stable oligonucleotide (-5 charge) was isolated per subunit. Structural analysis indicated that the sequence of the oligonucleotide is m7GpppGmpCp. Analysis of the mononucleotide fraction isolated by DEAE-Sephadex chromatography of the RNase T2 digest identified 15 to 23 internal N6-methyladenylic acid molecules per subunit.

Enzymatic basis for the selective inhibition of varicella-zoster virus by 5-halogenated analogues of deoxycytidine.

Dobersen, M J; Jerkofsky, M; Greer, S
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /11/1976 EN
Relevância na Pesquisa
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5-Bromodeoxycytidine (BrdC) and 5-iododeoxycytidine, at a concentration of 100 mug/ml, effectively inhibit the replication of varicella-zoster (VZ) virus in tissue culture. No toxicity could be demonstrated in uninfected cells under the same conditions. Studies on the enzymatic basis for this selective inhibition were undertaken. Infection of human embryonic lung cell monolayers with VZ virus-infected cells results in the induction of thymidine (dT), deoxycytidine (dC), and BrdC kinase activities (which are increased 10-, 40-, and 60-fold, respectively) and in a 70-fold stimulation in the incorporation of 3H nucleotide (5-bromodeoxyuridylate) derived from BrdC into DNA. The thermal stability of the VZ virus-induced activities differs significantly from the activities induced by herpes simplex virus type 1 and herpes simplex virus type 2 and those present in uninfected human embryonic lung cells. The VZ virus-induced dT, dC, and BrdC kinase are similarly affected by temperature and cofractionate upon Sephadex gel filtration, findings consistent with the hypothesis that these activities are the function of a single enzyme: a pyrimidine deoxyribonucleoside kinase. The molecular weight, calculated on the basis of the elution pattern on Sephadex G-150...

Isolation of Indole-3-ethanol Oxidase from Cucumber Seedlings 1

Vickery, Larry E.; Purves, William K.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /05/1972 EN
Relevância na Pesquisa
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Previous work in this laboratory has shown that cucumber (Cucumis sativus L.) seedlings contain large amounts, relative to other indolic compounds, of extractable indole-3-ethanol (IEt); tracer studies have established that IEt is metabolized to IAA. We have now succeeded in isolating an enzyme from these seedlings which catalyzes the oxidation of IEt to indole-3-acetaldehyde (IAAld). The identification of the product as IAAld was based on solvent partitioning of the free aldehyde and its bisulfite adduct and radiochromatography following incubation of enzyme with 14C-IEt. A novel, quantitative colorimetric test for IAAld was also developed utilizing the Salkowski reagent. Partial purification of the enzyme was achieved by salt gradient chromatography on Bio-Rex 70, heating the preparation to 70 C, and chromatography on Sephadex G-150. This purification procedure yielded an enzyme activity purified in excess of 3000-fold, and studies on a standardized Sephadex column suggest a molecular weight of the enzyme of approximately 105,000. The reaction was found to proceed only aerobically; and, in the absence of other electron acceptors, O2 appears to be reduced to H2O2. The enzyme has nearly maximum activity from pH 8 to 11.

Elevated serum levels of the eosinophil granule major basic protein in patients with eosinophilia.

Wassom, D L; Loegering, D A; Solley, G O; Moore, S B; Schooley, R T; Fauci, A S; Gleich, G J
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1981 EN
Relevância na Pesquisa
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A radioimmunoassay was established for the human eosinophil granule major basic protein (MBP). The mean level of MBP in sera from 105 normal control patients was 454 ng/ml, whereas in a sample of 188 patients with various forms of diseases, including the hypereosinophilic syndrome, levels as high as 14,000 ng/ml were measured. Serum levels of MBP did not correlate with eosinophil counts in normal subjects, but a positive correlation was seen in patients with eosinophilia; the patients with eosinophil counts greater than 350/mm3 generally showed increased levels of MBP. Many patients with skin disease and normal eosinophil counts had elevated levels of serum MBP. Monomer MBP has a molecular weight of 9,300, but in sera of patients with eosinophilia, the MBP activity was of high molecular weight, greater than 50,000. Analyses of serum by Sephadex G-200 and by electrofocusing suggest that MBP is not simply polymerized, but rather is bound to a larger carrier molecule. Monomeric MBP can be isolated from serum by reduction of serum with dithiothreitol, alkylation with iodoacetamide, and acidification to pH 2 followed by fractionation on Sephadex G-50 at pH 2. Under these conditions, up to 80% of the MBP emerges in monomeric form. The results indicate that eosinophil granule proteins circulate in blood covalently bound to serum proteins...

Sequence of Fibrinogen Proteolysis and Platelet Release after Intrauterine Infusion of Hypertonic Saline

Nossel, H. L.; Wasser, J.; Kaplan, K. L.; Lagamma, K. S.; Yudelman, I.; Canfield, R. E.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /11/1979 EN
Relevância na Pesquisa
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Plasma fibrinopeptide B (Bβ1-14 or FPB) immunoreactivity was studied by radioimmunoassay in patients who received intrauterine infusion of hypertonic saline to terminate pregnancy. FPB immunoreactivity increased with thrombin treatment (TIFPB) suggesting the presence of a larger FPB-containing peptide, since purified FPB is not altered by thrombin, whereas thrombin increases the immunoreactivity of Bβ1-42 (which includes FPB) 10-fold. TIFPB immunoreactivity in plasma, drawn 4 h after hypertonic saline infusion eluted from Sephadex G-50 similarly to isolated Bβ1-42. Streptokinase, incubated with normal plasma progressively generated TIFPB immunoreactivity, which showed a major component which eluted from Sephadex G-50 similarly to Bβ1-42. Streptokinase generated TIFPB much more rapidly in reptilase-treated plasma that contains fibrin I, (which still includes FPB), indicating that fibrin I is preferred over fibrinogen as a substrate for plasmin cleavage of arginine (Bβ42)-alanine (Bβ43). Serial studies were then made in 10 patients receiving intrauterine hypertonic saline. Fibrinopeptide A (FPA) levels rose immediately, reached a peak between 1 and 2 h, were declining at 4 h, and were normal at 24 and 48 h. TIFPB levels rose slightly in the 1st h...

Glucagon deficiency and hyperaminoacidemia after total pancreatectomy.

Boden, G; Master, R W; Rezvani, I; Palmer, J P; Lobe, T E; Owen, O E
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /03/1980 EN
Relevância na Pesquisa
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The first goal of this study was to investigate whether totally pancreatectomized patients are glucagon deficient and if so, to what degree. Immunoreactive glucagon (IRG) concentrations in peripheral plasma of nine pancreatectomized patients were not significantly different from those of 10 normal controls as measured by two antisera (30-K and RCS-5) both detecting the COOH-terminal portion of the molecule and one (RCS-5) postulated to be specific for pancreatic glucagon. Plasma from six of nine pancreatectomized patients were fractionated over Sephadex G-50 and IRG was measured with both antisera in the column eluates. Using 30-K, 80.8 +/- 9% of the IRG eluted within the void volume. This material was rechromatographed on Sephadex G-200 and found to have an apparent mol wt of approximately 200,000. Only 18.3 +/- 9% eluted in the IRG3500 region. IRG3500 was significantly reduced in pancreatectomized patients as compared to normal controls (49 +/- 9 vs. 18 +/- 9 pg/ml, P less than 0.05). Using RCS-5, all IRG (corresponding to 20 +/- 6 pg/ml of plasma) eluted in the IRG3500 region. The second goal of this study was to investigate the effects of chronic glucagon deficiency on plasma amino acids. In the nine pancreatectomized patients studied...