1. Structure-function studies of recombinant murine tripeptidyl-peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation
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Marete Hansen, Birgitta Tomkinson, and Wing-Fai Cheung
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Protein subunit ,Tripeptidyl-peptidase II ,Molecular Sequence Data ,Biophysics ,Aminopeptidases ,Biochemistry ,Cell Line ,law.invention ,Sepharose ,Mice ,Structure-Activity Relationship ,Structural Biology ,law ,Complementary DNA ,Endopeptidases ,Genetics ,Animals ,Humans ,Oligomerization ,Amino Acid Sequence ,Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ,Molecular Biology ,Subtilisin type ,chemistry.chemical_classification ,biology ,Alternative splicing ,Structure-function relationship ,Tripeptidyl peptidase II ,Complex formation ,Cell Biology ,Exopeptidase ,Recombinant Proteins ,Amino acid ,Serine protease ,Alternative Splicing ,chemistry ,Type C Phospholipases ,Recombinant DNA ,biology.protein - Abstract
Tripeptidyl-peptidase II (TPP II) is an exopeptidase with a remarkably high native Mr (> 106). Recently, an alternatively spliced, murine cDNA variant was identified which contains an additional 39 bp, encoding 13 aniino acids in the C- terminal end of the protein. The two enzyme variants were expressed in human kidney 293 cells. Both types of subunit were found to form the active oligomers. In addition, subunits containing the extra 13 amino acids formed an even larger complex eluting in the void volume of a Sepharose CL-4B column. Thus, it appears that this sequence is important for aggregation of subunits. © 1997 Federation of European Biochemical Societies.
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