[Isolation, purification and identification of metallothionein from strain BD102 of Hansenula anomala].
Metallothionein (MTs) in Cu and Cd resistant strain BD102 of Hansenula anomala were induced by administration of Cu2+ and Cd2+. These proteins were isolated and purified by Sephadex G-50 and subsequent DEAE-Sepharose CL-6B, then Sephadex G-25 for desalation. There were two isoform MTs by Cu(Cu-MTs), one form induced by Cd (Cd-MT). The molecular weights of the Cu-MTs and the Cd-MT were about 7 kD and 7.5 kD respectively. Exposure of Hansenula anomala to copper salts stimulated formation of two isoform Cu-MTs with a cysteine content of 6.6-6.8% and had 60 amino acids. Exposure of Hansenula anomala to cadmium, stimulated formation of Cd-MT with a cystein content of 10% was synthesized and had 61 amino acids. 4 atom Cu or Cd/mole MTs.
Lin
Z
Z
College of Life Sciences, Peking University, Beijing 100871, China.
Ma
G
G
Li
F
F
Shu
J
J
Chang
L
L
D000596:Amino Acids / Q000032:analysis; D019256:Cadmium Chloride / Q000494:pharmacology; D002148:Calmodulin-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D019327:Copper Sulfate / Q000494:pharmacology; D008668:Metallothionein / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D010843:Pichia / Q000378:metabolism*
D000596:Amino Acids; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins; C023548:copper-binding protein; D008668:Metallothionein; D019256:Cadmium Chloride; D019327:Copper Sulfate