On the Mechanism of Hemoglobin‐Haptoglobin Complex Formation

Pavlı́ček, Zdeněk; Jaenicke, Rainer

doi:10.1111/j.1432-1033.1971.tb01245.x

Cited by 6 publications

(4 citation statements)

References 15 publications

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“…Increased haptoglobin concentration within each sample will produce higher protein–protein (hemoglobin–haptoglobin) complexes, thus limiting the catalytically active species of the modified plate assay, producing reduced CL intensities. Previous studies verified the irreversible protein–protein binding with high specificity and marked changes in heme reactivity [34,35]. Indeed, eCL factor values were reduced significantly (t-test, p < 0.05) upon deterioration of milk quality for all particle sizes (e.g., values of 30.6 ± 0.8, 21.4 ± 1.9, and 14.6 ± 2.5 for milk-free assay, healthy, and clinical mastitis, respectively, using 25 nm cross-linked GNPs).…”

Section: Resultsmentioning

confidence: 81%

Gold Nanoparticle Size-Dependent Enhanced Chemiluminescence for Ultra-Sensitive Haptoglobin Biomarker Detection

Nirala

Shtenberg

2019

Biomolecules

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Bovine mastitis (BM) is a frequent disease in the dairy industry that causes staggering economical losses due to decreased milk production and increased health care costs. Traditionally, BM detection depends on the efficacy and reliability of analytical techniques that measure somatic cell counts (SCC), detect pathogens, and reveal inflammatory status. Herein, we demonstrate the detection of bovine haptoglobin, a well-documented acute phase protein for evaluating BM clinical status, by utilizing hemoglobin-binding capacity within luminol chemiluminescence (CL) system. The resulting haptoglobin–hemoglobin complex reduces the CL signal proportionally to inherent haptoglobin concentrations. Different sizes of cross-linked gold nanoparticles (GNPs) were examined for enhanced CL (eCL) signal amplification, presenting over 30-fold emitted radiation enhancement for optimized size within real milk samples with respect to nanoparticle-free assay. The eCL values were proportionally related to nanoparticle size and content, influenced by SCC and pathogen type (e.g., Escherichia coli and coagulase-negative staphylococci). The optimized bioassay showed a broad linear response (1 pg mL−1–10 µg mL−1) and minute detection limit of 0.19 pg mL−1, while presenting quantitative performance in agreement with commercial ELISA kit. Finally, the resulting optimized eCL concept offers an efficient label-free detection of haptoglobin biomarker, offering means to diagnose the severity of the associated diseases.

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Section: Resultsmentioning

confidence: 81%

Gold Nanoparticle Size-Dependent Enhanced Chemiluminescence for Ultra-Sensitive Haptoglobin Biomarker Detection

Nirala

Shtenberg

2019

Biomolecules

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“…It is reasonable to note that these two drugs are usually used under pathologic condition caused by infectious diseases. Also it is resulted that haptoglobin is an acute phase protein [15,16]. Furthermore, in vitro studies show that two antibiotics (especially ampicillin) may help Hp-Hb complex to remove hydrogen peroxide from serum.…”

Section: Resultsmentioning

confidence: 99%

Amplification of Antioxidant Activity of Haptoglobin(2-2)–Hemoglobin at Pathologic Temperature and Presence of Antibiotics

Tayari

Afsharzadeh

2011

Ind J Clin Biochem

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It is clear that Haptoglobin binds to Hemoglobin strongly and irreversibly. This binding, protects body tissues against heme-mediated oxidative tissue damages via peroxidase activity of Haptoglobin-Hemoglobin complex. Peroxidase activity of Haptoglobin(2-2)-Hemoglobin complex was determined via measurement of following increase in absorption of produced tetraguaiacol as the second substrate of Haptoglobin-Hemoglobin complex by UV-Vis spectrophotometer at 470 nm and 42°C. The results are showing that peroxidase activity of Haptoglobin(2-2)-Hemoglobin complex is modulated by homotropic effect of hydrogen peroxide as the allosteric substrate. On the other hand, antioxidant activity of Haptoglobin (2-2)-Hemoglobin is increased via heterotropic effect of two antibiotics (especially ampicillin) on the peroxidase activity of the complex. The condition of pathologic temperature along with the administration of ampicillin and/or coamoxiclav is in favor of amplification in antioxidant activity of Haptoglobin(2-2)-Hemoglobin and combating against free radicals in individuals with Hp2-2 phenotype. Therefore, oxidative stress effects have been diminished in the population with this phenotype.

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“…It is this easy loss of sialic acid that may well be responsible for the widely different estimates (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14) of the number of sialic acid residues per mole of H p 1-1 (28,29).…”

Section: Discussionmentioning

confidence: 99%

The Microheterogeneity of Human Haptoglobin and Its Complex with Hemoglobin

Yang¹,

Przybylska²

1973

Can. J. Biochem.

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and PRZYBYI.SKA, M. The microheterogeneity of human haptoglobin and its complex with hemoglobin. Can. J. Biochem. 51,597-685 ( 1973 ).Human haptoglobin, type 1s-IS, isolated from plasma and from ascites fluid was subjected to isoelectric focusing in polyacrylamide gel and its complex with horse cyaiaomethemoglobin was analyzed by isoelectric focusing in a column using a sucrose density gradient. Both methods revealed microheterogeneity. Similar patterns were obtained consisting of five to eight strong bands with a symmetrical distribution giving the highest yield in the center. An investigation of the nature of these bands was carried out and it was found that the sialic acid content varied in the different components. Experiments were undertaken to show that the multiple bands were not due to the binding of Ampholine to the protein and that this heterogeneity preexisted in haptoglobin prior to its isolation. No observable difference in heterogeneity was observed between samples of haptoglobin isolated by different methods and for complexes obtained by adding hemoglobin to haptoglobin and haptoglobin to hemoglobin.The unfractionated complex and the separated complex components were crystallized. YANG, N. J., et PRZYBYESKA, M. The microheterogeneity of human haptoglobin and its complex with hemoglobin. Can. J. Biochem. 51, 597-605 ( 1973 ). E'haptoglobine humaine de type IS-IS, isolCe du plasma et du liquide des ascites, est soumise la focalisation isoClectrique dans un gel de polyacrylamide et son complexe avec la cyano-mCthCmoglobine de cheval est analyst5 par focalisation isoCleetrique sur colonne, en prtsence d'un gradient de densit6 de saccharose. Les deux mCthodes rCvklent la microhCtCrog6nCitC. Les profils obtenus sont semblables et ils sont form& de einq B huit bandes importantes, distribuies de faqon symttrique, donnant un rendement plus ClevC dans le centre. La recherche de la nature de ces bandes nous a montrC que la teneur en acide sialique varie dans les diffCrents composCs. Des expCriences ont dCmontrC que les bandes multiples ne sont pas dues B la liaison de 1'Ampholine B la protCine et que cette httCrogCntit6 existait dCjB dans l'haptoglobine avant son isolation. Nsus n'avons observt aucune diECrence dans IVhCtCrogCnCitC entre les Cchantillons d'haptoglobine isolCe par diffCrentes mCthsdes et pour les complexes obtenus par addition d'hemoglobine B l'haptoglobine et d'haptoglobine h I'hCmoglobine. Le complexe non fractionnC et les constituants sCparCs du complexe sont cristallisCs. [Traduit par le journal]

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On the Mechanism of Hemoglobin‐Haptoglobin Complex Formation

Cited by 6 publications

References 15 publications

Gold Nanoparticle Size-Dependent Enhanced Chemiluminescence for Ultra-Sensitive Haptoglobin Biomarker Detection

Gold Nanoparticle Size-Dependent Enhanced Chemiluminescence for Ultra-Sensitive Haptoglobin Biomarker Detection

Amplification of Antioxidant Activity of Haptoglobin(2-2)–Hemoglobin at Pathologic Temperature and Presence of Antibiotics

The Microheterogeneity of Human Haptoglobin and Its Complex with Hemoglobin

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