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At least 613 records · Page 34Linked to original sources
PubMed1983

A new method of preparing hapten-carrier immunogens by coupling with Saccharomyces cerevisiae by periodate oxidation.

A new method of preparing hapten-carrier immunogens is described. The carrier used was Saccharomyces cerevisiae yeast. Coupling was carried out with bovine serum albumin (BSA). BSA was conjugated with mannose residues of Saccharomyces cerevisiae cell walls, following periodate oxidation to produce aldehyde groups reactive with side chain amino groups of BSA. The coupling was stabilized and non-reactant aldehydes were blocked with sodium borohydride reduction. A hapten, 3,5,3',5'-tetraiodo-L-tyrosyl-L-tyrosine, was also coupled with the yeast. Anti-hapten antibodies were obtained in rabbit with this conjugate.

Animals↗
PubMed1996

Daily changes in thyroid activity in the frog Rana perezi: variation with season.

Plasma triiodothyronine (T3) and thyroxine (T4) levels, as well as thyroid free (f) and bound (b) thyroid hormones (TH) content, were determined by radioimmunoassay (RIA) in adult Rana perezi frogs during a 24 h cycle in winter, spring, summer, and autumn. Significant daily changes in plasma T3 levels were present in all the seasons except for winter, being the lowest values observed during the scotophase. In contrast, plasma T4 only showed significant changes in spring, following a similar pattern to the one described for T3. Thyroid fT3 content did present day/night significant changes only in spring showing high contents at early scotophase. Mean fT4 content was higher at the beginning of light phase than during the rest of daily photocycle in spring and autumn, but significant differences appeared only in autumn. Regarding the thyroid bound content of TH, bT3, and bT4 presented significant daily changes in spring and autumn. However, different profiles were observed in these two seasons. High bound contents were found at early photo- and scotophase with lower values at late dark phase in spring, whereas higher contents were detected at this time in autumn. The present results indicate the existence of seasonally changing daily fluctuations in thyroid activity in Rana perezi and it seems that an interaction between photoperiod and temperature plays a role in the regulation of these daily changes.

Analysis of Variance↗
PubMed1990

Modulation of the renin-aldosterone system by iodotyrosines as tyrosine hydroxylase inhibitors.

This study shows that MIT and DIT stimulate aldosterone secretion. This may be due to their tyrosine hydroxylase inhibitory property. Dopamine abolishes the stimulation. Prolonged MIT administration enhances the stimulation of aldosterone secretion and can cause hypokalemia. Volume expansion reverses the hyperaldosteronism. PRA and blood pressure do not change, even after prolonged MIT intake.

Adult↗
PubMed2005

Preparation and testing of stationary phases and modified capillaries for affinity chromatography and affinity capillary electrophoresis of pepsin.

Three stationary phases have been prepared for affinity liquid chromatography isolation and separation of porcine and human pepsin. The phases contain 3,5-diiodo-L-tyrosine (DIT) bound to the supports HEMA BIO VS, HEMA BIO E and EPOXY TOYOPEARL. These phases have been tested on a model sample of porcine pepsin A and applied to human pepsin. Fractions have been collected and the chymase activity determined in selected analyses. For affinity CE, capillaries have been prepared by modifying the wall with 3-aminopropyltriethoxysilane, followed either by direct binding of DIT, or by binding L-tyrosine that was subsequently iodated. The dissociation constant K(d) has been determined for the pepsin-DIT complex from the changes in the electrophoretic mobilities.

Animals↗
PubMed2006

Protein radical formation on thyroid peroxidase during turnover as detected by immuno-spin trapping.

Thyroid peroxidase (TPO) is a 933 amino acid residue, heme-containing, integral membrane glycoprotein that catalyzes two steps in the maturation of the thyroid hormone precursor. As with other peroxidases, these reactions require hydrogen peroxide and initial enzyme oxidation. Previous researchers studied the oxidative state of the TPO heme moiety using spectrophotometric and catalytic analyses. We use a novel antiserum to 5,5-dimethyl-1-pyrroline N-oxide (DMPO) to detect radical-derived DMPO spin-trapped TPO. Our work reveals that TPO generates radical adducts in the presence of H2O2, but that the generation of these adducts can be suppressed by the addition of substrates and inhibitors. Chemical alteration of the tyrosine residues of TPO greatly reduces the generation of TPO-DMPO adducts. Iodide strongly suppresses the H2O2-generated production of TPO radical adducts and protects the enzyme from loss of enzyme activity. Because the normal catalytic mechanism of TPO involves the production of radical species, TPO is potentially more susceptible to oxidative damage than most enzymes which do not require H2O2 as a substrate. We hypothesize that oxidatively damaged TPO may trigger the production of anti-TPO autoantibodies, resulting in the development of autoimmune thyroid disorders. Evidence that correlates iodine deficiencies with development of thyroid autoimmune disorders supports this conjecture.

Amino Acids↗