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Results for “Enzyme Reactivators”

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PubMed2005

Time-dependent changes in antioxidant enzymes and vascular reactivity of aorta in streptozotocin-induced diabetic rats treated with curcumin.

In the present study changes in oxidative stress and vascular reactivity in aortic rings of chronic streptozotocin-diabetic (STZ-CON) and nondiabetic (ND-CON) rats is studied at 4 weekly intervals up to 24 weeks. The effect of chronic curcumin (200 mg/kg) treatment was also studied. Blood glucose and blood pressure levels were significantly higher in the STZ-CON group and curcumin administration had no significant effect on it. Superoxide dismutase and catalase activity were either unchanged or significantly increased during the early stage of diabetes whereas during the medium and late stage were significantly reduced. Reduced glutathione and lipid peroxidation levels significantly decreased as time after STZ administration increased. Phenylephrine (PE)-induced contraction was significantly (P < 0.05) increased during the early stage of diabetes, whereas it was significantly (P < 0.05) reduced at the medium and late stage of diabetes. Acetylcholine (Ach)-induced relaxation significantly decreased with respect to time after STZ administration. Sodium nitroprusside (SNP)-induced relaxation was unaltered up to initial stage but after medium stage there was a rightward shift and the pD2 value significantly decreased. Though curcumin treatment had no significant effect on superoxide dismutase, catalase, and reduced glutathione levels, it significantly reduced lipid peroxidation compared with diabetic control. Curcumin treatment attenuated the phenylephrine-induced increase in contraction during the early stage. However, curcumin treatment had no significant effect at the medium and late stage. Though curcumin administration improved Ach-induced relaxation it did not restore it to normal. Inability of curcumin to prevent oxidative stress during the late stage may be due to the fact that chronic diabetes (hyperglycemia) leads to excessive production of free radicals. Hence the present study shows that variations reported in antioxidant enzymes and vascular reactivity are due to the duration of diabetes or time after diabetes induction in STZ model and this can not be completely reversed by chronic treatment with curcumin.

Animals↗

PubMed1993

Inhibition kinetics of brain butyrylcholinesterase by Cd2+ and Zn2+, Ca2+ or Mg2+ reactivates the inhibited enzyme.

1. The inhibition kinetics of sheep brain butyrylcholinesterase (BChE) (acylcholine acylhydrolase, EC 3.1.1.8) by Cd2+ and Zn2+ has been studied. 2. KS has been determined as 0.14 mM. Cd2+ and Zn2+ were the hyperbolic mixed-type inhibitors of BChE. Ca2+ and Mg2+ had no effect on the enzyme activity in the experimental conditions. 3. But when the enzyme was inhibited by 0.1 mM Cd2+ or Zn2+, Ca2+ and Mg2+ reactivated the inhibited form of BChE.

Animals↗

PubMed1975

Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes.

The dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus which binds (tightly) only one tyrosyl adenylate or tyrosine per dimer is shown from kinetic, equilibrium dialysis, and gel filtration methods to have a second active site. ATP and tyrosine bind strongly and synergistically to the tyrosyl-tRNA synthetase tyrosyl adenylate complex, [E with Tyr similar to AMP], to give the complex [E with Tyr similar to AMP,ATP,Tyr]. This complex probably slowly forms an [E with (Tyr similar to AMP)2] complex which hydrolyses rapidly and does not accumulate. Similarly, the monomeric valyl-enzyme is shown to have two active sites. An [E with Val similar AMP,ATP,Val] complex is formed which probably slowly gives an unstable [E with Val similar AMP)2] complex. In view of this and the recent demonstrations that several aminoacyl-tRNA synthetases are composed of repeating sequences it is suggested that all of these enzymes have at least two active sites. The second site is difficult to detect by normal steady-state kinetic measurements and binding assays as these enzymes exhibit negative cooperativity of substrate binding hand half-of-the sites reactivity. A mechanism based on interacting sites is proposed that could account for these observations: changes in binding energy at one site may be coupled with catalysis at the other to give large rate enhancements. Howeever, this cannot account for the high specificity in the acylation of tRNA, A "VERIFICATION" PROCEDURE SEEMS ESSENTIAL. The proposed mechanism is quite general for catalysis and could be a reason why so many nonregulatory enzymes have subunits.

Adenosine Monophosphate↗

PubMed1973

Herpes simplex virus as a source of thymidine kinase for thymidine kinase-deficient mouse cells: suppression and reactivation of the viral enzyme.

Thymidine kinase (EC 2.7.1.21)-deficient mouse cells were infected with inactivated herpes simplex virus, after which "transformed" cells that produce viral thymidine kinase were isolated. Shortly after transformation, the expression of the viral enzyme could be suppressed and reactivated with high efficiency. On continued multiplication in nonselective medium, the proportion of cells producing the viral enzyme decayed exponentially. This decay seemed to represent a change in the expression of the viral gene for thymidine kinase rather than the loss of the gene from the cells, since the viral enzyme could be apparently reactivated in every cell, albeit at a very low frequency.

Aminopterin↗

PubMed1982

Comparison of simian and human cytomegalovirus reactivities in an enzyme-linked immunospecific assay: effect of antigen preparation on cross-reactive antigens.

Simian cytomegalovirus was substituted for human cytomegalovirus in an enzyme-linked immunoassay. Unlike the indirect immunofluorescence assay which demonstrates a two-way cross-reactivity, only one-way cross-reactivity was observed. Altering the method of simian antigen preparation gave some insight other this different reactivity.

Animals↗

PubMed1991

Mutation of a negatively charged amino acid in thioredoxin modifies its reactivity with chloroplastic enzymes.

A new over-expression system has been set up for Escherichia coli thioredoxin, yielding 55 mg purified protein/10 g fresh cells. This system has been used to produce thioredoxin modified by site-directed mutagenesis. Taking advantage of the structural and enzymatic similarity between E. coli and spinach m-type thioredoxin, Asp61 of E. coli thioredoxin has been changed into Asn in order to investigate the impact of the suppression of a charged residue on the interaction of thioredoxin with target enzymes. The modification did not significantly alter the structure of the protein. Neither the rate of reduction of insulin and 5,5'-dithio-bis(2-nitrobenzoic acid) by the reduced thioredoxin, nor the reduction by NADPH-dependent thioredoxin reductase, have been modified. The major effect of the mutation was observed for chloroplast enzyme activation with thioredoxin reduced by dithiothreitol and with thioredoxin reduced by ferredoxin-dependent thioredoxin reductase in a light-activation reconstituted chloroplast system. The substitution of the negatively charged Asp61 by the neutral Asn led to an increase in the efficiency of spinach fructose-1,6-bisphosphatase activation by the dithiothreitol-reduced thioredoxin, and to an increase in both spinach fructose-1,6-bisphosphatase and corn NADP-dependent malate dehydrogenase activities in the light-activation system. This suggests that the suppression of the negative charge improves the reactivity of thioredoxin with chloroplast enzymes such as fructose-1,6-bisphosphatase and ferredoxin-dependent thioredoxin reductase.

Amino Acid Sequence↗

PubMed2005

Reactivity of a new class of P450 enzyme models.

P450 enzyme models carrying a SO3(-) ligand coordinating to iron have been synthesized and characterized. These complexes show characteristics very similar to those of iron-heme cofactors of P450 enzymes. Their reactivity towards different reactions catalyzed by P450 enzymes such as epoxidation of double bonds, hydroxylation of non-activated C-H bonds, N-dealkylation of amines, and cleavage of diols (C-C-bond cleavage) has been investigated.

Computer Simulation↗

PubMed2000

Antioxidant enzyme expression and reactive oxygen species damage in prostatic intraepithelial neoplasia and cancer.

BACKGROUND: Oxidative stress results in damage to cellular structures and has been linked to many diseases, including cancer. The authors sought to determine whether the expression of three major antioxidant enzymes, copper-zinc superoxide dismutase (SOD1), manganese superoxide dismutase (SOD2), and catalase, was altered in human prostate carcinoma and its likely precursor, high grade prostatic intraepithelial neoplasia (PIN). The level of reactive oxygen species damage was evaluated by measuring the expression of the DNA adduct 8-hydroxydeoxyguanosine. METHODS: The authors evaluated the tissue expression of the antioxidant enzymes in prostate carcinoma by immunohistochemistry, immunogold electron microscopy, and enzymatic assay. The polymerase chain reaction was used to amplify and screen tissue specimens for the genes of SOD1, SOD2, and extracellular SOD (SOD3). Matched paraffin embedded tissue sections were evaluated by RNA in situ hybridization for expression of SOD1 and immunohistochemically for the DNA adduct 8-hydroxydeoxyguanosine. RESULTS: All prostatic tissues, including cancer, displayed immunoreactivity for the three antioxidant enzymes in epithelial cells, with no staining of the stroma, inflammatory cells, or endothelial cells. The number of immunoreactive cells was greater in benign epithelium than in PIN and cancer for each enzyme. The mean percentage and intensity of immunoreactive cells was greatest for SOD2, intermediate for SOD1, and lower for catalase. Staining in cancer was heterogeneous. Immunogold ultrasound studies revealed strong mitochondrial labeling for SOD2, which was greater in benign epithelium than in cancer; SOD1 labeling was invariably weaker, with nuclear labeling in benign epithelium and cytoplasmic labeling in cancer cells. There was no difference in enzyme activity for the three antioxidant enzymes between benign epithelium and cancer. No mutations were found in the 5 exons of SOD1, 5 exons of SOD2, and 3 exons of SOD3, except for 3 of 20 cases with polymorphisms for exon 3 of SOD1. Intense nuclear immunoreactivity for 8-hydroxydeoxyguanosine was present in fewer than 3% of epithelial cells, with no apparent differences among benign epithelium, PIN, and cancer. CONCLUSIONS: SOD1, SOD2, and catalase had lower expression in PIN and prostate carcinoma than in benign epithelium. The number of immunoreactive cells in PIN was similar to cancer, indicating that these are closely related. Enzyme activities were variable, with no difference between benign epithelial cells and cancer, although this lack of change in enzyme activity could have been due to the presence of contaminating benign cells within the cancer specimens. The results of reactive oxygen species damage were found only in the epithelium and not in the stroma. Expression of the DNA adduct 8-hydroxydeoxyguanosine was present in fewer than 3% of cells, with no apparent differences among benign epithelium, PIN, and cancer. These findings suggest that oxidative stress is an early event in carcinogenesis.

Aged↗

PubMed2000

Beta-galactoside alpha2,6 sialyltransferase in human colon cancer: contribution of multiple transcripts to regulation of enzyme activity and reactivity with Sambucus nigra agglutinin.

Colon cancer tissues display an increased activity of beta-galactoside alpha2,6 sialyltransferase (ST6Gal.I) and an increased reactivity with the lectin from Sambucus nigra (SNA), specific for alpha2,6-sialyl-linkages. Experimental and clinical studies indicate a contribution of these alterations to tumor progression, but their molecular bases are largely unknown. In many tissues, ST6Gal.I is transcriptionally regulated through the usage of different promoters that originate mRNAs diverging in the 5;-untranslated regions. RT-PCR analysis of 14 carcinoma samples, all expressing an increased ST6Gal.I enzyme activity, and of the corresponding normal mucosa revealed the presence of at least 2 transcripts. One, containing the 5;-untranslated exons, Y+Z, is thought to represent the "housekeeping" expression, and another previously described in hepatic tissues. Both the Y+Z and the hepatic transcripts were detectable in normal and cancer tissues but that latter form had a marked tendency to accumulate in cancer. The extent of alpha2,6-sialylation of glycoconjugates, as determined by SNA-dot blot analysis, was markedly enhanced in all cancer specimens, but the level of reactivity only partially correlated with the level of enzyme expression. Western blot analysis revealed a strikingly heterogeneous pattern of SNA reactivity among cancer tissues. These data indicate that: i) during neoplastic transformation of colonic cells, ST6Gal.I expression may be modulated through a differential promoter usage; ii) the extent of alpha2,6-sialylation of cancer cell membranes is not a direct function of the ST6Gal.I activity, strongly suggesting the existence of other, more complex mechanisms of regulation.

Aged↗

PubMed1976

Enzyme defense against reactive oxygen derivatives. II. Erythrocytes and tumor cells.

The enzymatic destruction of oxidizing products produced during metabolic reduction of oxygen in the cell (such as singlet oxygen, H2O2 and OH radical) involves the concerted action of superoxide dismutase-which removes O-2 and yields H2O2-and H2O2 removing enzymes such as catalase and glutathione peroxidase. A difference in distribution or ratio of these enzymes in various tissues may result in a different reactivity of oxygen radicals. It was found that in red blood cells superoxide dismutase and catalase are extracted in the same fraction as hemoglobin, while glutathione peroxidase appears to be "loosely" bound to the cellular structure. This suggests that in red blood cells catalase acts in series with superoxide dismutase against bursts of oxygen radicals formed from oxyhemoglobin, while glutathione & peroxidase may protect the cell membrane against low concentrations of H2O2. On the other hand, catalase activity is absent in various types of ascites tumor cells, while glutathione peroxidase and superoxide dismutase are found in the cytoplasm. However, the peroxidase/dismutase ratio is lower than in liver cells, and this may provide an explanation for the higher susceptibility of tumor cells to treatments likely to involve oxygen radicals.

Acetylcholinesterase↗

PubMed1997

How enzymes control the reactivity of adenosylcobalamin: effect on coenzyme binding and catalysis of mutations in the conserved histidine-aspartate pair of glutamate mutase.

Glutamate mutase is one of a group of adenosylcobalamin-dependent enzymes that catalyze unusual isomerizations that proceed through the formation of radical intermediates. It shares a structurally similar cobalamin-binding domain with methylcobalamin-dependent methionine synthase. In particular, both proteins contain the "DXHXXG" cobalamin-binding motif, in which the histidine provides the axial ligand to cobalt. The effects of mutating the conserved histidine and aspartate residues in methionine synthase have recently been described [Jarrett, J. T., Amaratunga, M., Drennan, C. L., Scholten, J. D., Sands, R. H., Ludwig, M. L., & Matthews, R. G. (1996) Biochemistry 35, 2464-2475]. Here, we describe how similar mutations in the "DXHXXG" motif of glutamate mutase affect coenzyme binding and catalysis in an adenosylcobalamin-dependent reaction. The mutations made in the MutS subunit of glutamate mutase were His16Gly, His16Gln, Asp14Asn, Asp14Glu, and Asp14Ala. All the mutations affect, in varying degrees, the rate of catalysis, the affinity of the protein for the coenzyme, and the coordination of cobalt. Mutations of either Asp14 or His16 decrease k(cat) by 1000-fold, and whereas cob(II)alamin accumulates as an intermediate in the wild-type enzyme, it does not accumulate in the mutants, suggesting the rate-determining step is altered. The apparent Kd for adenosylcobalamin is raised by about 50-fold when His16 is mutated and by 5-10-fold when Asp16 is mutated. There are extensive differences between the UV-visible spectra of wild-type and mutant holoenzymes, indicating that the mutant enzymes coordinate cobalt less well. Overall, the properties of these mutants differ quite markedly from those observed when similar mutations were introduced into methionine synthase.

Amino Acid Isomerases↗

PubMed1990

Herpes simplex virus type 1 ribonucleotide reductase: selective and synergistic inactivation by A1110U and its iron complex.

2-Acetylpyridine-5-[(dimethylamino)thiocarbonyl]thiocarbonohydr azone (A1110U) inactivated herpes simplex virus Type 1 ribonucleotide reductase (EC 1.17.4.1) by a first-order process (kinact) which had a maximum value (Mkinact) of 8 hr-1 and a Kd that was less than 1 microM. The stable complex between iron and A1110U, (A1110U)2Fe+i, inactivated this enzyme with a Mkinact of 7 hr-1 and a Kd of 7 microM. Free A1110U and its iron-complex synergized as inactivators of the enzyme. For example, the kinact for the combination of 2 microM A1110U and 1 microM (A1110U)2Fe+i as independent inactivators was calculated to be about 9 hr-1, while the observed value was 32 hr-1. The bimolecular rate constant for inactivation of the viral enzyme by (A1110U)2Fe+i in the presence of a saturating concentration of A1110U was 2.5 10(7) M-1 hr-1 at 30 degrees. Human ribonucleotide reductase was less sensitive to the inhibitory effects of A1110U and its iron-complex. This enzyme was neither inhibited nor inactivated by A1110U and was weakly inhibited by (A1110U)2Fe+i. Furthermore, inactivation required the combination of A1110U and (A1110U)2Fe+i. The bimolecular rate constant for inactivation of human ribonucleotide reductase by (A1110U)2Fe+i in the presence of a saturating concentration of A1110U was considerably smaller (3.8 10(6) M-1 hr-1 at 37 degrees) than the analogous constant for the viral enzyme. Several iron-chelating reagents with unrelated structures substituted for free A1110U in its various roles with both enzymes. However, the iron complexes of these alternative chelators did not substitute for (A1110U)2Fe+i. The rates of inactivation of both enzymes were independent of the oxidation state of iron in (A1110U)2Fe+i and of CDP concentration. The inactivated enzymes were reactivated rapidly by FeSO4, but were not reactivated by CoCl2, CuSO4, or NiCl2. MnCl2 inhibited reactivation of the viral enzyme by FeSO4.

Adenosine Triphosphate↗

PubMed1983

Reversibility characteristics of glucose-induced trehalase activation associated with the breaking of dormancy in yeast ascospores.

The breaking of dormancy in yeast ascospores by addition of glucose is associated with a sudden tenfold increase in the activity of trehalase. The rapid activation of trehalase is followed by a slower inactivation process which is greatly retarded in the presence of nitrogen sources and cycloheximide. When glucose is washed away from the spores after some time and the spores resuspended in glucose-free medium, the trehalase activity decreases sharply. Subsequent addition of new glucose partially reactivates the enzyme. The extent of reactivation decreases further with each subsequent activation/inactivation step. Changing the duration of the inactivation periods has no effect on this diminution of the reversibility. However, prolonging the duration of the activation step speeds up the loss of reversibility. On the other hand, addition of a nitrogen source or cycloheximide completely prevents the loss of reversibility. The results of the reversibility studies are in agreement with the phosphorylation mechanism which has been proposed for the underlying molecular process of trehalase activation. Apparently, they are also in agreement with proteolytic breakdown being responsible for the inactivation of trehalase after its initial activation. However, the effect of cycloheximide and nitrogen sources, at least in ascospores, does not appear to be due to inhibition or repression of protease synthesis, respectively, since the addition in the presence of glucose of a nitrogen source after trehalase inactivation immediately reactivates the enzyme completely.

Ascomycota↗

PubMed2000

Effects of beta-carotene on antioxidant enzyme activity, intracellular reactive oxygen and membrane integrity within post confluent Caco-2 intestinal cells.

As encountered with a plethora of other natural products, the antioxidant activity of beta-carotene has been proposed as one of the mechanisms by which diets rich in this pro-vitamin A active carotenoid apparently afford chemoprevention. Here, we report the ability of beta-carotene to alter endogenous reactive oxygen levels and antioxidant defences within non-stressed 'differentiated' monolayers of an intestinal epithelial cell line (Caco-2) and to subsequently effect resistance to general oxidative insult. The differentiated monolayers efficiently absorbed beta-carotene. Between 3 and 8 days post confluence, cultures exhibited a progressive increase in antioxidant enzyme activity and a corresponding reduction to intracellular ROS levels. The profile for antioxidant enzyme activity was unaffected by sustained daily supplementation with beta-carotene. However, after two daily treatments with 50 microM beta-carotene intracellular ROS levels were significantly reduced and there was a trend towards reduced intracellular ROS within monolayers subject to five daily treatments with 0.5 and 5 microM beta-carotene. Prolonged supplementation with 0.1 and 0.5 microM beta-carotene or short supplementation periods with 5 and 50 microM beta-carotene did not alter susceptibility to H(2)O(2). However, cultures treated daily between 3 and 8 days post confluence with 5 or 50 microM beta-carotene exhibited enhanced LDH release, increased non-adherence and enhanced Trypan blue staining when challenged with 10 mM H(2)O(2). In the absence of H(2)O(2), the beta-carotene treatments were not overtly toxic to the monolayers. These results indicate that beta-carotene does not enhance antioxidant defences within Caco-2 monolayers. The enhancement of H(2)O(2) toxicity by persistent, high doses of beta-carotene may contribute to the failure of this carotenoid to protect high risk individuals from certain degenerative conditions.

Antioxidants↗

PubMed1984

Alternate substrates of dopamine beta-hydroxylase. II. Inhibition by benzyl cyanides and reactivation of inhibited enzyme.

Several ring-substituted benzyl cyanides lead to inactivation of dopamine beta-hydroxylase during catalysis. With m-hydroxybenzyl cyanide, maximal inactivation occurs when an enzyme group with a pK alpha of 6.0 +/- 0.2 is ionized (Colombo, G., Rajashekhar, B., Giedroc, D. P., and Villafranca, J.J. (1984) J. Biol. Chem. 259, 1593-1600). This paper reports studies conducted to determine the stability of inactivated dopamine beta-hydroxylase. Inactivation of the enzyme by m-hydroxybenzyl cyanide at pH 6.4 is halted by lowering the pH to approximately 5.0 with acetate, fumarate, pyridine, or phosphate buffer in the presence of tyramine. However, if tyramine is omitted, reactivation occurs. The extent of reactivation is dependent upon the final pH value and buffer used to adjust the pH. Reactivation is observed as the pH is lowered from 6.4 to below 5.7 with acetate, fumarate, or HCl. With phosphate, reactivation occurs at any pH value from 6.9 to 4.5 but is greater at lower pH values. Thus, inactivation and reactivation have opposite pH dependencies. Also, reactivation is dependent upon the elapsed time of inactivation. At early times, no reactivation is observed when phosphate is used to adjust the pH, but reactivation is observed later in the inactivation reaction. Reactivation to 100% of the original activity does not occur under these conditions. These data suggest at least two inactivation mechanisms by benzyl cyanides: 1) formation of a tightly bound or covalent adduct between dopamine beta-hydroxylase and enzyme-bound mandelonitrile (or a rearranged form of this molecule), and 2) reversible inhibition resulting from cyanide binding to enzyme-Cu2+. Studies with radiolabeled p-hydroxybenzyl cyanide as well as EPR studies of dopamine beta-hydroxylase-Cu2+ are reported in the following paper.

Adrenal Medulla↗

PubMed2004

[Effects of exogenous gamma-aminobutyric acid on antioxidant enzyme activity and reactive oxygen content in muskmelon seedlings under nutrient solution hypoxia stress].

The effects of exogenous gamma-aminobutyric acid (GABA) on antioxidant defense system and reactive oxygen species (ROS) in seedlings of two varieties with different resistance to hypoxia stress were studied under hypoxia stress in a nutrient solution culture system. The results showed that GABA treatments enhanced the activities of antioxidant enzyme including SOD (Fig. 1), POD (Fig. 2), CAT (Fig. 3), while the concentrations of H2O2 (Fig. 4), O(-.)2 (Fig. 5), MDA (Fig. 6) decreased under hypoxia stress. Among the treatments of three different GABA concentrations, the effect of 50 mmol/L GABA treatment was better than that of 25 mmol/L GABA and 100 mmol/L GABA treatments. The effect of treatment with GABA in "Dongfang xingguang" seedlings, which had stronger hypoxia-resistance to hypoxia stress, were better than that in "Xiyu No.1" seedlings which had lower hypoxia-resistance. It indicates that GABA treatment of exogenous spraying to leaves can increase the activities of antioxidant enzyme under the hypoxia stress and plays an important role in enhancing the resistance to hypoxia stress of muskmelon seedlings through keeping low ROS contents.

Antioxidants↗

PubMed1988

The applications of reactive dyes in enzyme and protein downstream processing.

Downstream processing of proteins is often a key factor in the overall process of satisfying product specifications and meeting current commercial demands. In this context, affinity chromatography and other techniques based on the affinity concept have revolutionized protein purification technology, although they have failed to demonstrate their broader applicability at the process scale. On the other hand, reactive dyes offer many advantages as pseudoaffinity media and in many occasions have successfully circumvented problems associated with conventional affinity ligands. The main features of reactive dyes include their broad spectrum of interaction with proteins, low cost, ready availability, high reactivity, ease of immobilization, and both biological and chemical stability. Consequently, dye-ligand media now find application in both analytical and process-scale purification of proteins by techniques such as low- and high-pressure performance affinity chromatography, affinity partitioning, and affinity precipitation.

Chemical Phenomena↗

PubMed1988

Development of a fast solid-phase enzyme immunoassay for C-reactive protein.

A fast sandwich enzyme immunoassay has been developed for C-reactive protein (CRP). This method can be used for screening CRP concentration in large numbers of samples providing a non precipitation, non agglutination and non radioactive alternative for assessment of human CRP. Advantages over previously reported CRP sandwich assays include: assay time was reduced from 4 1/2 h to 45 min, incubations were made at room temperature instead of 37 degrees C and serum dilutions required were 100-400 fold instead of 10000-20000 fold. Correlations were good with both nephelometry and phosphorylethanolamine binding assay. The 45% false positives found with the slide-latex anti C-reactive protein method were reduced to 0% by the use of the described method.

C-Reactive Protein↗