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At least 523 records · Page 29Linked to original sources
PubMed1977

Mechanism of interference by chelating agents and sucrose in radioimmunoassay of angiotensin I.

EDTA, 2,3-dimercaptopropanol and sucrose were shown by Scatchard analysis to interfere in the radioimmunoassay of angiotensin I by altering the affinity, but not the capacity, of antibody for antigen. It is stressed that when interfering reagents are present in samples the assay result must be obtained from a standard curve in which each standard contains the interfering reagent(s) at a similar concentration as present in each sample mixture.

Angiotensin II↗
PubMed1980

Effect of sulfhydryl reagents on the enzymatic activity of human renin: implications for renin assay.

Sulfhydryl (SH) reagents are sometimes used in renin assays, yet their effects on the enzymatic activity of human renin are not clearly understood. We have employed radioimmunoassay of angiotensin I (AI) to assess the effects of dithiothreitol (DTT) and of dimerecaptopropanol (DMP) on the formation of AI at pH 5.5 and at pH 7.4. When ethylenediamine tetra-acetate, phenylmethylsulfonyl fluoride, and 8-hydroxyquinoline were used as angiotensinase inhibitors, both DTT and DMP decreased the rate of AI formation in each of two human plasma pools at both pH values. In contrast, in a system of semi-purified human kidney renin and hog renin substrate, DTT enhanced the formation of AI, increasing Vmax without changing Km at both pH values. The reaction of human kidney renin with synthetic tetradecapeptide renin substrate was stimulated by DTT at pH 7.4 but inhibited by DTT at pH 5.5. In all three systems, SH reagents altered the ratio of reaction velocity at pH 5.5 to reaction velocity at pH 7.4. We conclude that SH reagents affect the assay of human renin in complex ways which depend upon the pH of incubation and upon the subcomplex ways which depend upon the pH in incubation and upon the substrate utilized. Although the mechanism of these effects is not known, such effects probably contribute to the lack of agreement among many of the procedures for renin assay.

Angiotensin I↗
PubMed1988

Synergistic actions of disulfide-reducing agents on 1-methyladenine-induced oocyte maturation in starfish.

Several disulfide-reducing agents, such as dithiothreitol, 2,3-dimercapto-1-propanol, cysteine ethyl ester, and cysteine methyl ester enhanced the effectiveness of 1-methyladenine (1-MeAde) to induce oocyte maturation in the starfish Asterina pectinifera. This enhancement occurred at relatively low concentrations at which these agents by themselves were ineffective in inducing oocyte maturation. The agents caused a marked (about twofold) increase in specific [1-3H]MeAde binding. The binding increased directly in relation to the potency of the agents in enhancing 1-MeAde action. Scatchard analysis indicated that dithiothreitol increased the Bmax without affecting the affinity of 1-MeAde binding. These results strongly suggest that disulfide-reducing agents enhance the maturational action of 1-MeAde by increasing the number of 1-MeAde binding sites in oocyte cortices.

Adenine↗
PubMed1983

Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain.

Antimycin, 2-nonyl-4-hydroxyquinoline N-oxide and funiculosin induce O.2(-) generation by submitochondrial particles oxidizing succinate, whereas KCN, mucidin, myxothiazol or 2,3-dimercaptopropanol inhibit O.2(-) generation. Thenoyltrifluoroacetone does not induce superoxide production by itself but slightly stimulates the reaction initiated by antimycin. The results indicate that auto-oxidation of unstable ubisemiquinone formed in centre o of the Q-cycle generates most of the O.2(-) radicals in the cytochrome bc1-site of the mitochondrial respiratory chain.

Alkenes↗
PubMed1978

Aspects of bradykinin radioimmunoassay.

125I-derivatives of Tyr1-kallidin, Tyr5-bradykinin, and Tyr8-bradykinin were prepared. A technique for purification of the monoiodinated derivative is described. Bradykinin antisera were tested for their ability to bind the mono-iodinated analogues. Each antiserum had a characteristic preference for one of the three labeled peptides. The sensitivity of each antiserum was greatest when it was used with the label bound most avidly by that antiserum. The specificity of an antiserum was not changed by varying the labeled analogue. Some common enzyme inhibitors had significant effects on the antigen-antibody reactions. Lecithin interfered with the reaction between antiserum and Tyr1-kallidin. The data suggest that antisera for bradykinin radioimmunoassay be tested with several radioactive iodobradykinins to maximize their usefulness. In addition, enzyme inhibitors used to stabilize levels of kinins in biological fluids should be tested for their effects on the assay. Biologic samples rich in lipid may give spurious radioimmunoassay results unless they are freed of those phospholipids that can bind labeled and unlabeled peptides.

Animals↗