Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin.

@article{Tomkinson1991CharacterizationOC,
  title={Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin.},
  author={Birgitta Tomkinson and Ari K. J{\'o}nsson},
  journal={Biochemistry},
  year={1991},
  volume={30 1},
  pages={168-74}
}
Tripeptidyl peptidase II is a high molecular weight serine exopeptidase, which has been purified from rat liver and human erythrocytes. Four clones, representing 4453 bp, or 90% of the mRNA of the human enzyme, have been isolated from two different cDNA libraries. One clone, designated A2, was obtained after screening a human B-lymphocyte cDNA library with a degenerated oligonucleotide mixture. The B-lymphocyte cDNA library and a cDNA library, obtained from human fibroblasts, were rescreened… CONTINUE READING