title: Chelatins in Euglena gracilis and Ochromonas danica.
abstract: Amino acid analysis was performed on low molecular weight copper binding proteins purified from two species of Protozoa after exposure to a high level of this metal. The compound from Ochromonas is similar to Cu-chelatins. The two peptides from Euglena have a different molecular weight and a very dissimilar amino acid composition. Peptide No. 1 has a peculiar composition with a high content of aspartic acid and arginine. Some speculations are made about its detoxification role in comparison with other compounds found in blue-green algae.
authors.forename: E
authors.initials: E
authors.lastname: Piccinni
authors.forename: O
authors.initials: O
authors.lastname: Coppellotti
authors.forename: L
authors.initials: L
authors.lastname: Guidolin
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000032:analysis; D005056:Euglena gracilis / Q000032:analysis*; D056890:Eukaryota / Q000032:analysis*; D008667:Metalloproteins / Q000302:isolation & purification*; D008970:Molecular Weight
chemical_list: D002352:Carrier Proteins; D008667:Metalloproteins; C016298:chelatin; C023548:copper-binding protein