Purification and partial characterization of ceruloplasmin from chicken serum

DiSilvestro, Robert A.; Harris, Edward D.

doi:10.1016/0003-9861(85)90568-5

Cited by 15 publications

(6 citation statements)

References 33 publications

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“…Ceruloplasmin (CP) in mammals is a plasma protein, which accumulates over 95% of the copper contained in plasma (Martinez‐Subiela, Tecles, & Ceron, ). When the copper concentration in the blood of birds is low, the serum level of CP is low as well (Disilvestro & Harris, ). Ceruloplasmin is a multifunctional protein, which stores, transports and transfers copper to cells owing to the presence of CP receptors.…”

Section: Discussionmentioning

confidence: 99%

The effect of feed supplementation with a copper‐glycine chelate and copper sulphate on selected humoral and cell‐mediated immune parameters, plasma superoxide dismutase activity, ceruloplasmin and cytokine concentration in broiler chickens

Jarosz

Marek

Grądzki

et al. 2017

Animal Physiology Nutrition

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SummaryThe varied bioavailability and different effects of organic forms of copper on the immune system of poultry have prompted the search for new feed additives based on copper compounds containing modified chelate complexes. The aim of the study was to determine the effect of inorganic and organic forms of copper on selected parame- K E Y W O R D Schicken, copper-glycine chelate, cytokine expression, flow cytometry, superoxide dismutase activity

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Section: Discussionmentioning

confidence: 99%

The effect of feed supplementation with a copper‐glycine chelate and copper sulphate on selected humoral and cell‐mediated immune parameters, plasma superoxide dismutase activity, ceruloplasmin and cytokine concentration in broiler chickens

Jarosz

Marek

Grądzki

et al. 2017

Animal Physiology Nutrition

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“…Caeruloplasmin isolated from chick serum contains 4 copper atoms per molecule (DiSilvestro & Harris, 1985). On the other hand, albumin (from bovine sources) has been shown by Scatchard analysis to have two independent binding sites for copper (Mohanakrishnan & Chignell, 1982).…”

Section: Discussionmentioning

confidence: 99%

“…Purification of chicken caeruloplasmin used a modification of the procedure described by DiSilvestro & Harris (1985), designed for rapid purification with small samples. Briefly, solid (NH4)2SO4 was slowly dissolved in serum to 25 % saturation of 4°C, followed by centrifugation.…”

Section: Preparation Of Chicken Caeruloplasminmentioning

confidence: 99%

Regulation of aortic CuZn-superoxide dismutase with copper. Caeruloplasmin and albumin re-activate and transfer copper to the enzyme in culture

Dameron

Harris

1987

Biochemical Journal

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Caeruloplasmin and albumin were compared as potential donors of copper to Cu2Zn2-superoxide dismutase (CuZn-SOD) in culture. Aortas from 15-day copper-deficient chicks were suspended in oxygenated, serum-free, Waymouth medium (752/1) for 24 h. SOD activity was restored when the medium was supplemented with CuCl2, a copper-albumin complex or caeruloplasmin, all present at a level equivalent to 5 microM-copper. Activation did not occur at 4 degrees C or with Cu-EDTA as the supplement. Mn2+ and Zn2+, alone or in combination, did not activate nor enhance the activation achieved by CuCl2. The activation with CuCl2 was not inhibited by cycloheximide or cordycepin. [67Cu]Caeruloplasmin and albumin when added to the medium transferred radioactive copper to at least three cytosolic protein fractions, one of which was determined by immunoprecipitation to be CuZn-SOD. The transfer of 67Cu from caeruloplasmin was inhibited by increasing amounts of unlabelled caeruloplasmin; disodium EDTA (1.0 mM) had no effect on the transfer of copper from caeruloplasmin. These data show that aortic SOD activity, suppressed in copper deficiency, can be restored by incubating the aortas in culture medium supplemented with copper salts. In this system, caeruloplasmin and Cu-albumin appear equally capable of activating aortic CuZn-SOD. Moreover, the transfer of copper into the enzyme structure appears to be the primary event restoring catalytic activity to the enzyme.

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“…The difference in response may be attributable to the eliciting cause or the immunoassay methods employed; it is notable that the earlier report by Upragarin ( 2005 ) of large increases in SAA concentration used chicken-specific antibodies. In chickens, ceruloplasmin ( Cp ) is constitutively present, but at lower concentrations than observed in mammals (Disilvestro and Harris, 1985 ). Cp is considered a minor APP in chickens, with basal concentrations ranging from 0.03 to 0.12 g/L, increasing 2 to 3-fold during an APR (Disilvestro and Harris, 1985 ; Richards and Augustine, 1988 ; Georgieva et al, 2010 ; Najafi et al, 2015a ).…”

Section: Introductionmentioning

confidence: 99%

A comparative study of acute-phase protein concentrations in historical and modern broiler breeding lines

2018

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Acute-phase proteins (APP) are secreted from the liver as a result of inflammation or infection and are measurable in serum and plasma. To determine whether the constitutive APP serum amyloid A (SAA), alpha-1-acid glycoprotein (AGP), ceruloplasmin (Cp), and ovotransferrin (Ovt) have changed as a result of selection for improved production and growth characteristics over the last 40 yr two historical broilers lines were compared to a modern line of the same lineage. Serum was harvested from blood samples taken from the 3 broiler lines on days 10, 17, and 20, and the APP concentrations were determined using immunoassay methods. Most of the significant changes observed were age related, with SAA and Cp having significantly lower concentrations at day 20 than days 10 and 17 in all lines. The only significant difference between lines was observed at day 20 on which both Cp (P = 0.01) and AGP (P = 0.03) were significantly higher in the modern line than the 90s line, though no significant differences were noted between the modern and 70s line. When evaluating the difference in APP concentrations between males (Cx) and females (Px) across all 3 lines, females had a higher SAA at day 17 and lower SAA at day 20, P = 0.0078 and 0.0327 respectively, and males had a significantly higher Ovt on days 17 and 20 (P = 0.0002 and P = 0.003 respectively). These results reveal that APP concentrations fluctuate over this early period of growth and that the changes in APP serum concentration appear uniform between 3 lines with very contrasting selection history, suggesting the improvements made in meat production efficiency since the 1970s have not affected the circulating concentrations of these constitutively expressed APP.

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Purification and partial characterization of ceruloplasmin from chicken serum

Cited by 15 publications

References 33 publications

The effect of feed supplementation with a copper‐glycine chelate and copper sulphate on selected humoral and cell‐mediated immune parameters, plasma superoxide dismutase activity, ceruloplasmin and cytokine concentration in broiler chickens

The effect of feed supplementation with a copper‐glycine chelate and copper sulphate on selected humoral and cell‐mediated immune parameters, plasma superoxide dismutase activity, ceruloplasmin and cytokine concentration in broiler chickens

Regulation of aortic CuZn-superoxide dismutase with copper. Caeruloplasmin and albumin re-activate and transfer copper to the enzyme in culture

A comparative study of acute-phase protein concentrations in historical and modern broiler breeding lines

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