Isolation and partial characterization of a cadmium-binding protein from the American oyster (Crassostrea virginica)

Ridlington, James W.; Fowler, Bruce A.

doi:10.1016/0009-2797(79)90041-3

Cited by 120 publications

(34 citation statements)

References 12 publications

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“…8). Finally, if the protein is concentrated, desalted, and frozen prior to spectral analysis, there is usually a reduction of the 250/280 nm ratio to about 2:1 as previously reported (1). The 250/280 nm ratio also may be reduced greatly by lowering the pH to 2.0, which releases the Cd from the protein, resulting in loss of the Cd-S chromophore in a manner similar to mammalian MT.…”

Section: Spectral Studiesmentioning

confidence: 77%

“…Previous studies from a number of laboratories (1)(2)(3)(4)(5)(6)(7)(8)(9)(10) have demonstrated the presence of cadmium-binding proteins (CdBP) in marine molluscs with properties that are both similar to and different from mammalian methallothionein (MT) (11,12). As previously noted (11), basic research on nonmammalian metal-binding proteins is of great potential value in elucidating not only the evolutionary pathway(s) of MT but also in gaining insight into its as yet unknown normal biological function.…”

Section: Introductionmentioning

confidence: 98%

“…As previously noted (11), basic research on nonmammalian metal-binding proteins is of great potential value in elucidating not only the evolutionary pathway(s) of MT but also in gaining insight into its as yet unknown normal biological function. In addition, since these proteins permit marine food organisms such as oysters to bioaccumulate toxic metals such as cadmium, they are also of practical interest with respect to In a first report (1), the American oyster, Crassostrea virginica, was found to produce a low molecular metalbinding protein in response to cadmium exposure. This protein, which was isolated via Sephadex G-75 column chromatography followed by DEAE-anion-exchange chromatography using an NaCl step gradient, was found to have a lower cysteine content than MT and contain aromatic amino acids.…”

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization Studies of Cadmium-Binding Proteins from the American Oyster, Crassostrea virginica

Fowler¹,

Engel²,

Brouwer³

1986

Environmental Health Perspectives

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The previously reported low molecular weight cadmium-binding protein (CdBP) from the American oyster, Crassostrea virginica, has been further purified and characterized by improved technical methods. The internal organ distribution ofthe protein within the oyster and effects of life cycle/season on CdBP production also have been evaluated. CdBP isolated by extended ion-exchange gradients or double ion-exchange chromatography followed by HPLC analysis possesses an electrophoretic R,of about 0.7 and contains relatively little Zn, as previously reported. Cysteine, lysine, and glycine are the dominant amino acids. When ionexchange columns are developed with NaCl gradients, the aromatic residues tryptophan, tyrosine, and phenylalanine are found to be present, but these may be largely removed depending upon whether the protein is denatured and carboxymethylated prior to analysis. The ultraviolent absorption spectrum of CdBP also was variable, with 250/280 nm ratios ranging from 17:1 immediately after ion-exchange chromatography to 2:1 following concentration procedures. Internal organ distribution studies showed that the visceral mass contained most of the Cd present with lesser amounts in the gills and mantle. In contrast with mammals, CdBP accounts for only about 30%o of the total cell Cd burden in these tissues. Cu displacement of Cd from the protein is a particular problem during the summer spawning season and appears to stem from altered Cu metabolism during this period. Relative oyster dormancy during the winter also reduces CdBP production in response to Cd, and the protein is obtained most readily during the fall and spring. In summary, CdBP shares both similarities and differences with MT, and the magnitude of these parameters depends greatly on both the biology of the oyster and technical procedures used to isolate/characterize the protein.

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Section: Spectral Studiesmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization Studies of Cadmium-Binding Proteins from the American Oyster, Crassostrea virginica

Fowler¹,

Engel²,

Brouwer³

1986

Environmental Health Perspectives

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“…Since the first report of metallothioneins, the metal-binding proteins, in equine renal cortex (Margoshes and Vallee, 1957) and their later purification and characterisation (Kagi and Vallee, 1960), these proteins have been found in a wide range of animals (White and Rainbow, 1986;Aoki and Suzuki, 1984;Suzuki et at., 1980;Kohler and Riisgard, 1982;Ridlington and Fowler, 1979;Rochet al, 1982;Webb, 1979;Elinder et al, 1987). However, it was not until 1980 that the existence of metal binding proteins was first reported in higher plants (Rauser and Curvetto, 1980).…”

Section: Introductionmentioning

confidence: 99%

Accumulated forms of thallium and cadmium inLemna minor. II. Relationship between duration of exposure and metal-protein binding

Kwan

Smith

1990

Chemical Speciation & Bioavailability

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Gel filtration chromatography (with Sephadex G25, G50 and G100) was used to separate the different forms of thallium (TI) and cadmium (Cd) in the cytosol fraction of Lemna minor and to examine the influence of the duration of metal exposure on the speciation of the two elements. A major proportion of Cd in the soluble phase was found to be bound to three groups of proteinaceous and polypeptide fractions; two of these, the high molecular weight protein fraction (Mr > 150,000) and the low polypeptide sized moieties of about Mr 1,SOO or less were constitutive entities, whereas the intermediate sized fraction (Mr 7,000-8,000) could only be detected in plants previously exposed to Cd. After 12 days of exposure to Cd this fraction accounted for the greatest part of the bound Cd in Lemna tissues. Extending the period of exposure from 18 hours to 12 days resulted in a shift in the distribution of Cd between the low and intermediate fractions. Evidence for Tl-protein binding was limited and confined to the high molecular weight fraction, and most of the Tl in the soluble phase was present in a form closely allied to the free ion. The contrasting behaviour between the two elements has been interpreted in terms of the differences in their physicochemical properties.

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“…The characterization of the form of cadmium in the oysters is essential for interpreting the results of the epidemiological study. There have been several reports on the form of cadmium in shellfish (13)(14)(15)(16)(17). However, most of these studies have been performed after exposure of collected shellfish to different concentrations of cadmium.…”

Section: Introductionmentioning

confidence: 99%

Characterization Studies on the Cadmium-Binding Proteins from Two Species of New Zealand Oysters

Nordberg¹,

Nuottaniemi²,

Cherian³

et al. 1986

Environmental Health Perspectives

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Isolation and partial characterization of a cadmium-binding protein from the American oyster (Crassostrea virginica)

Cited by 120 publications

References 12 publications

Purification and Characterization Studies of Cadmium-Binding Proteins from the American Oyster, Crassostrea virginica

Purification and Characterization Studies of Cadmium-Binding Proteins from the American Oyster, Crassostrea virginica

Accumulated forms of thallium and cadmium inLemna minor. II. Relationship between duration of exposure and metal-protein binding

Characterization Studies on the Cadmium-Binding Proteins from Two Species of New Zealand Oysters

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