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Search results for: Anti rabbit Antithrombin Whole IgG from antiserum

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Rapid and simple isolation procedure for lipoprotein lipase from human milk.

Lipoprotein lipase (LPL) is an important enzyme in lipid and energy metabolism of all vertebrates. Measurement of its activity in human postheparin plasma has become a standard procedure for diagnosis of Type I hyperlipoproteinemia and other types of hypertriglyceridemias. This paper presents a rapid and simple purification procedure for human lipoprotein lipase and the production of specific polyclonal antibodies. In the isolation procedure, the fat moiety of human milk obtained by centrifugation was delipidated and a buffer-extractable fraction chromatographed sequentially on heparin-Sepharose and phenyl-Sepharose. This three-step procedure provides a high yield of apparently pure LPL with very high specific activity against radiolabeled triacylglycerol substrates. The apparent molecular weight of LPL on SDS-PAGE was 60 kDa. Amino acid analysis and NH2-terminal sequencing proved the identity and the apparent homogeneity of the isolated enzyme. alpha-Lactoferrin and antithrombin III, common contaminants in earlier isolation procedures, were not detectable immunologically. Purified LPL was used to produce in the rabbit a specific polyclonal antiserum that inhibited LPL activity from human postheparin plasma and other tissues. In postheparin plasma from normal individuals, anti-LPL IgG was used in Western blotting to show LPL protein. In preheparin plasma, or in certain patients with Type I hyperlipoproteinemia, no specific signal was detected. The improved purification procedure presented here allows the rapid isolation of human LPL and production of antibodies to the protein, both of which will greatly facilitate future studies of this important enzyme.
R Zechner

2538 related Products with: Rapid and simple isolation procedure for lipoprotein lipase from human milk.

0.1 mg0.1 mg1 mg400Tests20 ug0.1 mg200 10 200 500 10ìg1 mg

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Novel platelet-agglutinating protein from a thrombotic thrombocytopenic purpura plasma.

A novel platelet-agglutinating protein (PAP) was purified approximately 2,000-fold from the plasma of a patient with thrombotic thrombocytopenic purpura (TTP) by ammonium sulfate fractionation, DEAE-Sephacel and concanavalin A-Sepharose chromatographies. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with and without reduction, this preparation revealed a major protein band with a molecular weight of 37,000, and a minor band with a molecular weight of 32,000-34,000. After elution from the gel, only the 37,000-mol wt protein corresponding to the major band induced the platelet agglutination. When four normal plasmas and the recovery plasma from the same TTP patient were subjected to the similar purification steps, the 37,000-mol wt major band was absent. The 125I-PAP bound to the platelets in a concentration-dependent manner. The platelet agglutination induced by PAP was not inhibited by hirudin, heparin in the presence of antithrombin III, phenylmethylsulfonyl fluoride, apyrase, aspirin, or prostaglandin I2. However, it was inhibited by IgG from normal adults and from the same TTP patient after recovery. The anti-37,000-mol wt PAP antiserum prepared in the rabbit formed a single precipitin line against the highly purified PAP. Using this antiserum in the Western immunoblotting, the 37,000-mol wt protein band was found in the three TTP plasmas, of which the platelet-agglutinating activity was inhibited by the anti-37,000-mol wt PAP IgG. The 37,000-mol wt immunoprecipitin band was absent in the plasmas obtained from another two TTP patients, two normal subjects, two patients with idiopathic thrombocytopenic purpura, and two patients with disseminated intravascular coagulation. These results suggest that the 37,000-mol wt PAP is present only in certain cases of TTP, and is likely to be responsible for the formation of platelet thrombi in the microcirculation.
F A Siddiqui, E C Lian

1629 related Products with: Novel platelet-agglutinating protein from a thrombotic thrombocytopenic purpura plasma.

1.0mg96T1mg0.05 mg96T 50 UG1.0mg1 Set100ug100 μg100ug100ug Lyophilized

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alpha2-Macroglobulin on human vascular endothelium.

alpha2-Macroglobulin (alpha2M) has been identified on the luminal surface of endothelial cells in sections of normal human arteries, veins, and lymphatics by the indirect immunofluorescent technique. The specificity of the immunofluorescent reaction was confirmed by immunoabsorption studies. Prior absorption of the anti-alpha2M antiserum by purified alpha2M at equivalence completely inhibited endothelial surface as well as hepatic parenchymal cell staining. Endothelial cells in blood vessels were not stained when sections were treated with rabbit antisera toward alpha1-antitrypsin, antithrombin III, IgG, IgA, IgM, C3, or fibrinogen. The location of alpha2M at the surface of the vessel wall suggests that this protease inhibitor may protect the vascular endothelium from potentially injurious intravascular proteases.
C G Becker, P C Harpel

2295 related Products with: alpha2-Macroglobulin on human vascular endothelium.

96tests 100ul2 1 ml2ug2ug1 mg100.00 ug10 μg100 μg 100ul100.00 ug

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