Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin

Essamadi, Abdel Khalid; Bengoumi, Mohammed; Zaoui, Driss; Faye, Bernard; Bellenchi, Gian Carlo; Musci, Giovani; Calabrese, Lilia

doi:10.1016/s1096-4959(02)00030-1

Cited by 8 publications

(6 citation statements)

References 22 publications

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“…The molecular weight of second peak (B) as a source of ceruloplasmin was determined by gel filtration chromatography using sephadex G-200 column (3 x 98) cm calibrated with known molecular weight proteins that were listed in Table (2 138111) dalton. This finding was in a good agreement with the previous results where it was reported that the molecular weight of ceruloplasmin was (130000-135000) dalton from serum of normal individual (Noyer et al, 1980;Ehrenwald and Fox, 1994;Essamadi et al, 2002).…”

Section: Molecular Weight Determination Of Cp By Gel Filtrationsupporting

confidence: 93%

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Partial Separation and Some Kinetic Studies of Ceruloplasmin in Human Serum

Ahmad¹,

Al-Helaly²

2009

RJS

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The study attempts to isolate the enzyme ceruloplasmin from human serum. Two proteinous components had been isolated by gel filtration chromatography from the precipitate produced by polyethylene glycol (4000). It was found that only the second peak had a high activity for ceruloplasmin. The apparent molecular weight of the isolated ceruloplasmin using gel filtration chromatography and SDS-PAGE was ( 138111) and (134400) dalton respectively.Maximum activity for ceruloplasmin was obtained using (35.8) mmol/l of pphenylenediamine as a substrate for the enzyme, sodium acetate (0.1 mol/l) as a buffer at pH (5.45) for ( 35) minutes at (56) °C. Using lineweaver-burk plot, it was found that maximum velocity (V max ) and Michaelis constant (K m ) had the values of (0.83) µmol/ min and (15.38) mmol/l respectively. The effects of some chemical compounds on the ceruloplasmin activity were investigated. Sodium chloride showed uncompetitive inhibition on the activity of the enzyme at a concentration of (70) mmol/l.

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Section: Molecular Weight Determination Of Cp By Gel Filtrationsupporting

confidence: 93%

“…Ceruloplasmin has been purified, from human plasma (Noyer et al, 1980), camel (Essamadi et al, 2002), sheep (Calabrese et al,1983), dolphin (Bonaccorsi et al, 1992 and others. In this research the ceruloplasmin was isolated from normal human serum.…”

Section: Results and Discussion Precipitation Of The Proteinmentioning

confidence: 99%

Partial Separation and Some Kinetic Studies of Ceruloplasmin in Human Serum

Ahmad¹,

Al-Helaly²

2009

RJS

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“…Ceruloplasmin has aroused interest for many years due to its redox potential displaying oxidant or antioxidant properties according to environmental conditions (27). The purification of Cp from various plasma sources (human, camel, bovine, horse, rat, chicken, goose, and rat) was described in the literatures (28,29,30,31,32,33,34,35). The present study describes a simple human Cp partial purification protocol including ammonium sulfate, dialysis and gel filtration with sephacryl -S200 to the sera of CRF patient and healthy subject.…”

Section: Discussionmentioning

confidence: 99%

Estimation Activity and Partial Purification of Ceruloplasmin from Sera of Patients with Chronic Renal Failure and Healthy Subjects

Zainal¹

2014

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CeruloplasminCP (EC1.16.3.1) activity has been assayed in (32) serum samples of patients with Chronic Renal Failure CRF, and (32) serum samples of healthy individuals without any clinically detectable diseases have been used as control group. The aim of this study is to measure CP activity and partially purifying the enzyme from sera of patients with CRF and healthy individuals. The results of this study revealed that CP activity of patient's serum shows a highly significant decrease (p < 0.05) compared to that of the healthy individuals. Ceruloplasmin enzyme was partially purified from the serum of patient with CRF and and healthy individual by three steps which operates throughout under mild conditions 4°, acetate buffer (pH 6.8): First step including the use of ammonium sulfate precipitation, second step utilize dialysis with acetate buffer, while the third step consists of gel-filtration on Sephacryl S200(27×1.6cm) . Insufficiently purified ceruloplasmin fractions obtained at various stages are diluted to the appropriate ionic strength and re-utilized. Two proteinous components had been isolated by gel filtration chromatography from the supernatant produced by ammonium sulfate.

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“…The purification of Cp from various plasma sources (human, camel, bovine, horse, rat, chicken, goose, and rat) was described in the literatures (Linder and Moor, 1977;Essamadi et al, 2002;Calabrese et al, 1981;Calabrese et al, 1988;Hilewicz-Grabska et al, 1988;Okumura et al, 1991;Ehrenwald and Fox 1994). The presence of a complex of Cp with lactoferrin in breast milk was also reported (Sokolov et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…The presence of a complex of Cp with lactoferrin in breast milk was also reported (Sokolov et al, 2006). Adult and young camel Cp were isolated and purified using the Single-step chromatography on amino ethyl-activated Sepharose (Essamadi et al, 2002). However, most common purification steps of Cp include ammonium sulfate precipitation, and a series of tedious chromatographic steps such as anion-exchange chromatography, size-exclusion chromatography, and hydrophobic chromatography.…”

Section: Introductionmentioning

confidence: 99%

A novel and one-step purification of human ceruloplasmin by acharan sulfate affinity chromatography

et al. 2009

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Human ceruloplasmin, a copper binding alpha(2)-glycoprotein, was purified by a single-step procedure using acharan sulfate affinity chromatography. Acharan sulfate was immobilized to amine-functionalized agarose matrix through carboxylic acids. Ceruloplasmin in human plasma was obtained from 0.4 M NaCl salt elution and characterized by SDS-PAGE (132 and 125 kDa), isoelectric focusing (pI 4.6), Western blotting, and MALDI-TOF-MS peptide mass fingerprinting. Ceruloplasmin was purified 106 fold with a specific oxidase activity of 0.53 U/mg protein.

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Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin

Cited by 8 publications

References 22 publications

Partial Separation and Some Kinetic Studies of Ceruloplasmin in Human Serum

Partial Separation and Some Kinetic Studies of Ceruloplasmin in Human Serum

Estimation Activity and Partial Purification of Ceruloplasmin from Sera of Patients with Chronic Renal Failure and Healthy Subjects

A novel and one-step purification of human ceruloplasmin by acharan sulfate affinity chromatography

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