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

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.

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).

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

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

scholarly journals Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by Surface Plasmon Resonance (BiaCore)

2011 ◽  
Vol 105 (06) ◽  
pp. 1053-1059 ◽  
Author(s):  
Berhane Ghebrehiwet ◽  
Kusumam Joseph ◽  
Alice Kao ◽  
Khalil Bdeir ◽  
Douglas Cines ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Endothelial Cell ◽  
High Molecular Weight ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Proteins ◽  
Binding Protein ◽  
High Molecular Weight Kininogen ◽  
Cell Binding

SummaryThe physiologic activation of the plasma kallikrein-kinin system requires the assembly of its constituents on a cell membrane. High-molecular-weight kininogen (HK) and cleaved HK (HKa) both interact with at least three endothelial cell binding proteins: urokinase plasminogen activator receptor (uPAR), globular C1q receptor (gC1qR,) and cytokeratin 1 (CK1). The affinity of HK and HKa for endothelial cells are KD=7–52 nM. The contribution of each protein is unknown. We examined the direct binding of HK and HKa to the soluble extracellular form of uPAR (suPAR), gC1qR and CK1 using surface plasmon resonance. Each binding protein linked to a CM-5 chip and the association, dissociation and KD (equilibrium constant) were measured. The interaction of HK and HKa with each binding protein was zinc-dependent. The affinity for HK and HKa was gC1qR>CK1>suPAR, indicating that gC1qR is dominant for binding. The affinity for HKa compared to HK was the same for gC1qR, 2.6-fold tighter for CK1 but 53-fold tighter for suPAR. Complex between binding proteins was only observed between gC1qR and CK1 indicating that a binary CK1-gC1qR complex can form independently of kininogen. Although suPAR has the weakest affinity of the three binding proteins, it is the only one that distinguished between HK and HKa. This finding indicates that uPAR may be a key membrane binding protein for differential binding and signalling between the cleaved and uncleaved forms of kininogen. The role of CK1 and gC1qR may be to initially bind HK to the membrane surface before productive cleavage to HKa.

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