From Tetrahymena thermophila （strain BF5）, the coding region of Cd-MT gene was cloned and sequenced. and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separ...From Tetrahymena thermophila （strain BF5）, the coding region of Cd-MT gene was cloned and sequenced. and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts （Part 1：7-61; Part 2：64-118; Part 3：122-162）. The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.展开更多
通过室内急性暴露实验研究了翡翠贻贝（Perna viridis）消化腺富集Cu及其MTLP（metallothionein like protein）水平随时间的变化规律．结果表明，2种Cu浓度暴露条件下（12．7μg／L和63．5μg／L），贻贝消化腺内Cu的平均吸收速率分别...通过室内急性暴露实验研究了翡翠贻贝（Perna viridis）消化腺富集Cu及其MTLP（metallothionein like protein）水平随时间的变化规律．结果表明，2种Cu浓度暴露条件下（12．7μg／L和63．5μg／L），贻贝消化腺内Cu的平均吸收速率分别为2．045和7．028μg·（g·d）^-1，富集系数分别为2074和1619．实验测定了所有样本的溶解态Cu与总Cu含量，2个暴露组二者的比值随时间呈现出不同的变化趋势，低浓度组先降低随后上升到与对照样本几乎相同的水平，而高浓度组一直呈下降趋势，表明不同污染程度生物体内金属消化机制进程存在差异．利用Brdicka极谱法测定了贻贝消化腺内MTLP的含量，对照组贻贝消化腺的MTLP平均含量为（0．551±0．037）ms／g；12．7μg／L Cu暴露组MTLP含量随时间的变化范围是0．407～0．699ms／g，而63．5μg／L Cu暴露组在暴露初始MTLP水平就显著增加（P〈0．001），变化范围由初始0．942mg／g降至0．826mg／g．分析结果表明贻贝消化腺内的MTLP水平随着水体及生物体内的金属含量升高而增加，并与体内Cu浓度成明显的负指数增长关系（P〈0．0001）．展开更多
文摘From Tetrahymena thermophila （strain BF5）, the coding region of Cd-MT gene was cloned and sequenced. and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts （Part 1：7-61; Part 2：64-118; Part 3：122-162）. The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.
