scholarly journals Isolation of (copper, zinc-) thioneins from pig liver

1976 ◽  
Vol 155 (3) ◽  
pp. 631-635 ◽  
Author(s):  
I Bremner ◽  
B W Young
Keyword(s):  
Binding Proteins ◽  
Copper Binding ◽  
Pig Liver ◽  
Total Metal ◽  
Copper Zinc ◽  
Metal Ratio ◽  
Copper Binding Proteins

The copper-binding proteins with mol. wt. of approx. 12000 in the cytosol of pig liver have been identified as copper-thioneins. They contain variable amounts of zinc, with approx. 10% total metal in the protein. The molar cysteine/metal ratio is approx. 2:1.

Rapid induction of copper-binding proteins in the gills of metal exposed mussels

1980 ◽  
Vol 67 (2) ◽  
pp. 215-218 ◽  
Author(s):  
A. Viarengo ◽  
M. Pertica ◽  
G. Mancinelli ◽  
G. Zanicchi ◽  
M. Orunesu
Keyword(s):  
Binding Proteins ◽  
Copper Binding ◽  
Rapid Induction ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins in the plasma of winter flounder (Pseudopleuronectes americanus)

1980 ◽  
Vol 58 (4) ◽  
pp. 609-613 ◽  
Author(s):  
P. E. Fletcher ◽  
G. L. Fletcher
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Egg Yolk ◽  
Winter Flounder ◽  
Zinc Binding ◽  
Copper Binding ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins were isolated from the plasma of winter flounder using gel filtration chromatography. A single copper-binding protein fraction of molecular weight 170 000 was isolated from the plasma of both sexes.In male and female flounder over 95% of the plasma zinc was associated with a zinc-binding protein(s) with a molecular weight of 76 000. In male flounder the remaining zinc appeared to be bound to a protein(s) of molecular weight 186 000. In female flounder the remaining 5% of the zinc was associated with two zinc-binding fractions with apparent molecular weights of 186 000 and 340 000 – 370 000.Extracts of plasma vitellogenin and egg yolk proteins revealed significant quantities of zinc and copper. It is hypothesized that the female specific zinc-binding protein (340 000 – 370 000) was vitellogenin.

Stability and Folding of Copper-Binding Proteins

2010 ◽  
pp. 61-80
Author(s):  
Irina Pozdnyakova ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Binding Proteins ◽  
Copper Binding ◽  
Copper Binding Proteins

High molecular weight zinc- and copper-binding proteins in the liver of the rat; Effect of centrifugation

1987 ◽  
Vol 135 (2) ◽  
pp. 129-132
Author(s):  
J.B. Dielhof, ◽  
J.G. Van Der Enden, ◽  
TH.M.W. Stolk ◽  
C.J.A. Van Den Hamer,
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Binding Proteins ◽  
Copper Binding ◽  
Copper Binding Proteins

Isolation of copper-binding proteins from activated sludge culture

2001 ◽  
Vol 44 (2-3) ◽  
pp. 453-459 ◽  
Author(s):  
K. Fukushi ◽  
S. Kato ◽  
T. Antsuki ◽  
T. Omura
Keyword(s):  
Molecular Weight ◽  
Activated Sludge ◽  
Metal Uptake ◽  
Binding Proteins ◽  
Growth Media ◽  
Copper Binding ◽  
Molecular Weights ◽  
Binding Capability ◽  
Copper Binding Proteins

Six copper-binding microbial proteins were isolated from activated sludge cultures grown on media containing copper at various concentrations. Molecular weights among isolated proteins were ranged from 1.3k to 174k dalton. Isolated proteins were compared for their copper binding capabilities. Proteins isolated from cultures grown in the presence of copper in the growth media exhibited higher copper binding capabilities than those isolated from the culture grown in the absence of copper. The highest metal uptake of 61.23 (mol copper/mol protein) was observed by a protein isolated from a culture grown with copper at a concentration of 0.25 mM. This isolated protein (CBP2) had a molecular weight of 24k dalton. Other protein exhibited copper binding capability of 4.8-32.5 (mol copper/mol protein).

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