Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

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

Monica Nordberg, Iris Nuottaniemi, M. George Cherian, Gunnar F. Nordberg, Tord Kjellström and Justine S. Garvey
Environmental Health Perspectives
Vol. 65 (Mar., 1986), pp. 57-62
DOI: 10.2307/3430163
Stable URL: http://www.jstor.org/stable/3430163
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Characterization Studies on the Cadmium-Binding Proteins from Two Species of New Zealand Oysters
Preview not available

Abstract

Two different types of New Zealand oysters-Ostrea lutaria (OL) and Crassostrea glomerata (CG)-contained different concentrations of zinc, copper, and cadmium. OL oysters had 5.3 μg Cd/g, 3.4 μg Cu/g, 100 μg Zn/g; CG oysters had 1.4 μg Cd/g and 936 μg Zn/g. Both kinds of oysters were shown by gel filtration (G-75) to contain cadmium and zinc in fractions corresponding to a high molecular weight protein (corresponding to the size of albumin or larger) which was heat labile. OL oysters contained cadmium in fractions corresponding to a molecular weight of approximately 6500. The cadmium-binding protein in these fractions was heat-stable. This protein contained no detectable amounts of zinc and was not present in the CG oysters. Further purification by gel filtration (G-50) was performed to obtain a purer protein fraction. Isoelectric focusing of the protein obtained by G-50 filtration showed one main fraction of protein with a pI ∼ 5.9 at ∼ 13°C. CG oysters contained cadmium and zinc in a polypeptide with low molecular weight (MW 1000). The cadmium-binding oyster proteins are minimally reactive in a competitive binding radioimmunoassay in comparison to the reactivity of a typical vertebrate metallothionein; the proteins may be metallothioneins, but, if so, they do not exhibit the principal determinants characteristic of vertebrate metallothioneins.

Page Thumbnails

  • Thumbnail: Page 
[57]
    [57]
  • Thumbnail: Page 
58
    58
  • Thumbnail: Page 
59
    59
  • Thumbnail: Page 
60
    60
  • Thumbnail: Page 
61
    61
  • Thumbnail: Page 
62
    62