摘要
A small amount of heavy metal binding protein,identified by BioRad Protein Assay,has been iso-lated from the adult brine shrimp,Artemia franciscanus.This protein has an apparent molecular weight be-tween 6000 to 9000 dalton.a UV absorption peak at 260 instead of 280 nm like most proteins;andhas high affinity towards binding with radioactive labeled <sup>109</sup>Cd.These characteristics are similarto that of metallothioneins reported for many vertebrate and invertebrate,marine and terrestrialanimals.After the brine shrimp is exposed to a small amount of Cd<sup>2+</sup>for 24 h,a large amount ofmetallothionein can be isolated,showing the inducibility of this detoxifying protein in the adult Artemiain a short period of time.
A small amount of heavy metal binding protein, identified by BioRad Protein Assay, has been isolated from the adult brine shrimp, Artemia franciscanus. This protein has an apparent molecular weight between 6000 to 9000 dalton. a UV absorption peak at 260 instead of 280 run like most proteins; andhas high affinity towards binding with radioactive labeled 109Cd. These characteristics are similar to that of metallothioneins reported for many vertebrate and invertebrate, marine and terrestrial animals. After the brine shrimp is exposed to a small amount of Cd for 24 h, a large amount of metallothionein can be isolated, showing the inducibility of this detoxifying protein in the adult Artemia in a short period of time.
