Coordination catalysis: The oxidation of amino acids and peptides by dioxygen in the presence of transition metal ions

1983 ◽  
Vol 79 ◽  
pp. 259-260
Author(s):  
A. Dempsey ◽  
D.A. Phipps
2016 ◽  
Vol 327-328 ◽  
pp. 55-69 ◽  
Author(s):  
Maurizio Remelli ◽  
Valeria M. Nurchi ◽  
Joanna I. Lachowicz ◽  
Serenella Medici ◽  
M. Antonietta Zoroddu ◽  
...  

1970 ◽  
Vol 27 (4) ◽  
pp. 701-714 ◽  
Author(s):  
C. H. Castell ◽  
Barbara Smith ◽  
Wanda Neal

The addition of 10–50 ppm of several transition metal ions rapidly decreased the extractable protein content of blended fish muscle. The most active metals were Cu++ and Cr++ followed by Sn++ and Cd++. Other ions tested, Ce++, Zn++, Ni++, Co++, Fe++, Fe+++, V++, and Mn++, brought about relatively little or no change in extractable protein nitrogen (EPN) values. Effects of the metals differed with muscle from different species. Lean fish were more susceptible than either fatty fish or shellfish. Of all the species tested the metals had the least effect on scallops. A limited number of tests indicated that fish that were badly emaciated through starvation were more susceptible to the metal-induced change than normal individuals of the species.Addition of certain amino acids, notably cysteine, histidine, glutamic acid, and tryptophane, protected the muscle against metal-induced reduction of EPN. With lean fish, the amino acids that protected the muscle against metal-induced change in the protein also protected it against metal-induced oxidation of the lipids; with fatty fish, protection against rancidity was somewhat less; the invertebrates seemed to be normally protected against both without the addition of amino acids. This natural immunity of marine invertebrate muscle to changes induced by the addition of heavy metal ions may in part be attributed to their normally high content of free amino acids.


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