Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase.
Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase.
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人糖基天冬酰胺酶 cDNA 的克隆和序列分析。
DOI：
10.1016/0014-5793(90)81211-6
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发表时间：
1990
期刊：
影响因子：
3.5
通讯作者：
AronsonJr,NN
中科院分区：
文献类型：
--
作者：
Fisher,KJ;Tollersrud,OK;AronsonJr,NN
我们使用含有大鼠肝天冬酰胺酶基因序列的221-bp PCR扩增片段分离了人胎盘糖基天冬酰胺酶的全长cDNA（HPAsn.6）。从人克隆中推导的氨基酸序列显示出与大鼠酶的α和β亚基的序列同一性。人类酶编码为34.6 kDa多肽，其经后处理产生约1.5 kDa的两个亚基。19.5（α）和15（β）kDa。电荷富集区存在于发生裂解的预测位点。使用抗大鼠肝天冬酰胺酶α和β亚基的多克隆抗体，我们已经证明人酶在结构上与大鼠酶相似。
We have isolated a full‐length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221‐bp PCR amplified fragment containing rat liver asparaginase gene sequences. The deduced amino acid sequence from the human clone showed sequence identity to both the α and β subunits of the rat enzyme. The human enzyme is encoded as a 34.6 kDa polypeptide that is post‐translationally processed to generate two subunits of approx. 19.5 (α) and 15 (β) kDa. A charge enriched region is present at the predicted site where cleavage occurs. Using polyclonal antibodies against the α and β subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.