Amino acid composition of cadmium-binding protein induced in a marine diatom,Phaeodactylum tricornutum

1989 ◽  
Vol 43 (3) ◽  
pp. 394-401 ◽  
Author(s):  
Y. Maita ◽  
S. Kawaguchi
1979 ◽  
Vol 183 (3) ◽  
pp. 683-690 ◽  
Author(s):  
H Ohtake ◽  
M Koga

Zn-binding protein in liver of the partially hepatectomized rat was purified by column chromatography on Sephadex G-75 and DEAE-cellulose. Homogeneity was judged by polyacrylamide-disc-gel electrophoresis. The molecular weight determined by gel-permeation chromatography in 6 M-guanidine hydrochloride was 6700. This value is in good agreement with the molecular weight calculated from the amino acid composition, which was 6073. Zn-binding protein was composed of 61 amino acid residues, and the distinctive features include an extremely high content of cysteine, which accounted for one-third of the total amino acid residues, and an absolute absence of aromatic amino acids as well as of histidine, leucine and arginine. The amino acid composition was similar to that of the metallothioneins previously isolated from rat liver and mouse liver. These observations suggest that the Zn-binding protein can be classified as a type of metallothionein. Zn-binding protein contained 8.2g-atoms of zinc per mol and traces of copper, but no cadmium. The molar ratio of thiol groups to zinc was calculated to be 2.5:1. Possible roles of this Zn-binding protein in the transport and storage of zinc in the liver are discussed.


1973 ◽  
Vol 58 (3) ◽  
pp. 421-423 ◽  
Author(s):  
J. G. HEATHCOTE ◽  
R. J. WASHINGTON

SUMMARY Preliminary analysis of the zinc-binding protein isolated from the human benign hypertrophic prostate gland was carried out using a micro method. The most interesting feature of the amino acid composition of the protein hydrolysate appears to be the large molar proportion of histidine which is present. This might account for the binding of divalent cations.


2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton

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