Isolation and characterization of a basic carboxypeptidase from human seminal plasma.

@article{Skidgel1988IsolationAC,
  title={Isolation and characterization of a basic carboxypeptidase from human seminal plasma.},
  author={Randal A. Skidgel and Peter A Deddish and Rick M. Davis},
  journal={Archives of biochemistry and biophysics},
  year={1988},
  volume={267 2},
  pages={660-7}
}
A carboxypeptidase which cleaves the C-terminal arginine or lysine from peptides was purified by a two-step procedure; gel filtration on Sephacryl S-300 and affinity chromatography on arginine-Sepharose. The activity increased 280% after the first step, indicating the removal of an inhibitor from the crude starting material. The activity in the crude seminal plasma eluted from the Sephacryl S-300 column with an apparent Mr 98,000 and after purification with an Mr 67,000, indicating that it… CONTINUE READING