| Abstract |
A cadmium-binding protein was purified the cell-free extract of extreme cadmium tolerant Hansenula anomala B-7. The molecular weight was determined to be approximately 33,000 and was composed two kinds of subunits having a molecular weight of 18,000 and 14,000, respectively. The extinction coefficient E^1%_280 nm of the cadmium-binding protein was calculated to be 19.58. The amount of cadmium in the cadmium-binding protein was 9.26㎍ per 100㎍ of protein. A total of 14 amino acids were detected in the cadmium-binding protein, including aspartic acid, glycine and alanine that were present in a high quantity, but proline, valine and methionine were not found. The purified cadmium-binding protein contained a high quantity of cysteine and cadmium, and therefore this protein showed clearly the characteristics of metallothionein. |
