A spectrophotometric method for estimating hemin in biological systems

Lombardo, Maria Elisa; Araujo, Lidia Susana; Ciccarelli, Alejandra; Batlle, Alcira

doi:10.1016/j.ab.2004.11.002

Cited by 43 publications

(34 citation statements)

References 10 publications

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“…A battery of experiments was carried out to validate an analytical methodology to quantify total Fe from blood meal product using UV−visible properties reported elsewhere. 26 The first attempt was thought to determine both the working Fe concentration and the more reliable wavelength. Several diluted solutions were prepared from a stock solution of 10 g product·L −1 to cover an Fe concentration up to 28 mg Fe·L −1 (0.28, 0.55, 1.10, 2.75, 5.50, 8.25, 11.0, and 27.5 mg Fe·L −1 ).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Blood Meal-Based Compound. Good Choice as Iron Fertilizer for Organic Farming

Yunta

Foggia

Bellido-Díaz

et al. 2013

J. Agric. Food Chem.

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Prevention of iron chlorosis with Fe synthetic chelates is a widespread agronomical practice but implies high costs and environmental risks. Blood meal is one of the main fertilizers allowed to be used in organic farming. Through this work a novel blood meal fertilizer was audited. Measurements such as FTIR, Raman, electron paramagnetic resonance, and Mössbauer spectroscopy, UV-visible properties, stability against pH, and batch experiments were performed to characterize and assess the reactivity on soil constituents and agronomic soils. The spectroscopy findings give clear indications that Fe is in the ferric oxidation state, is hexacoordinated, and has a low-spin form suggesting a similar structure to hemin and hematin. A spectrophotometric method at 400 nm was validated to quantify blood meal concentration at low electrolyte concentrations. Batch experiments demonstrated high reactivity of blood meal fertilizer with soil constituents, mainly in the presence of calcium, where aggregation processes are predominant, and its ability to take Fe from synthetic Fe (hydr)oxides. The beneficial profile of blood meal by a providing nitrogen source together with the capability to keep the Fe bound to porphyrin organic compounds makes it a good candidate to be used as Fe fertilizer in organic farming.

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Section: ■ Materials and Methodsmentioning

confidence: 99%

Blood Meal-Based Compound. Good Choice as Iron Fertilizer for Organic Farming

Yunta

Foggia

Bellido-Díaz

et al. 2013

J. Agric. Food Chem.

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“…Detailed procedures have been described elsewhere [29,30]. We applied a simple method for heme isolation according to Egyed's method [30].…”

Section: Purification Of Hemementioning

confidence: 99%

Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: Possible mechanism of action

Khodarahmi

Soori

Karimi

2009

International Journal of Biological Macromolecules

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“…-0.60 mM SDS and HbS interaction, are depictive of dimerized heme [75] and soluble hemin [67] respectively with their ratios depicting the predominant species in the reaction set up [76]. Besides, peaks between 365 and 370 nm also occurred for the spectral depiction of the [Ca 2?…”

Section: Discussionmentioning

confidence: 99%

“…to the HbS Soret regions shows that the 40 lM Ca 2? spectrum is associated with two peaks: a 397 nm peak, which suggests hemin formation [66,67] and a smaller 430 nm synonymous with deoxyHb conformation [41,68]. The 0.20 lM Ca 2?…”

Section: Discussionmentioning

confidence: 99%

“…in the presence of 5.0 mM SDS. These 365-370 nm peaks reflect the formation of dimerized heme species [62,75] while the peaks between 381 and 398 nm represent soluble hemin [66,67] as expulsed iron-protoporphyrin (FP)-IX [77,78]. The implication is that interactions with depictive spectrum or spectra with enhanced 365-370 nm peaks as compared to 381-398 nm would have expulsed and sequestered heme, thus cutting down on the potential toxicities of the liberated hemes and vice versa.…”

Section: Discussionmentioning

confidence: 99%

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Cation Modulation of Hemoglobin Interaction with Sodium n-Dodecyl Sulfate (SDS). II: Calcium Modulation at pH 5.0

Nwamba

Chilaka

Moosavi-Movahedi

2011

Cell Biochem Biophys

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We investigate the conformational differences between HbA and HbS in the presence and absence of Ca(2+) concentrations (0-40 μM) akin to those within the erythrocyte cytoplasm and the membrane mimetic and native structure disrupting environments of the Plasmodium parasite food vacuole at pH 5.0. The experiments were monitored by UV-Vis spectrophotometery in the range of 250-650 nm. Our results suggest that the HbS, on interacting with both the membrane mimic and 40 μM Ca(2+), undergoes an "expansion" akin to the burst phase of proteins accompanied by tyrosine exposure while that of the HbA occurred with tryptophan exposure. Our results suggest conformational flexibility in the HbS unlike in the HbA. Besides, the spectral results also suggest that the HbS complexes with the Ca(2+) in its immediate environment without strain (due to its inherent conformational flexibility), unlike the HbA, thus appropriating the cation from its vicinity. The implications of these results are discussed in the light of possible mechanisms employed by the HbS to resist protease digestion or at least slow down the kinetics of the protease activities and on how these same factors can predispose the homozygous HbS individuals to sickling and consequent vaso-occlusive crisis.

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A spectrophotometric method for estimating hemin in biological systems

Cited by 43 publications

References 10 publications

Blood Meal-Based Compound. Good Choice as Iron Fertilizer for Organic Farming

Blood Meal-Based Compound. Good Choice as Iron Fertilizer for Organic Farming

Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: Possible mechanism of action

Cation Modulation of Hemoglobin Interaction with Sodium n-Dodecyl Sulfate (SDS). II: Calcium Modulation at pH 5.0

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