Cloning and sequence analysis of a cDNA for human glycosylasparaginase

FEBS Letters

Tollersrud, Ole K.¹  Fisher, Krishna J.¹  Aronson, Nathan N.¹ 

[1] Department of Molecular and Cell Biology, Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

关键词: Glycosylasparaginase;    Lysosome;    cDNA;    Aspartylglucosaminuria;    Glycoprotein degradation;   

DOI  :  10.1016/0014-5793(90)81211-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown