Further characterization of porcine kidney aminoacylase I reveals close similarity to 'renal dipeptidase'.

@article{Heese1988FurtherCO,
  title={Further characterization of porcine kidney aminoacylase I reveals close similarity to 'renal dipeptidase'.},
  author={D Heese and H. G. L{\"o}ffler and Karlheinrich R{\"o}hm},
  journal={Biological chemistry Hoppe-Seyler},
  year={1988},
  volume={369 7},
  pages={559-66}
}
We present data indicating that aminoacylase I (EC 3.5.1.14) from porcine kidney and 'renal dipeptidase' (EC 3.4.13.11) are closely related. We show that, in situ, a considerable fraction of aminoacylase activity ist attached to membranes. Incubation of washed microsomal membranes with phospholipase C from B. cereus results in the rapid solubilization of aminoacylase I, suggesting that aminoacylase--as shown for renal dipeptidase before--bears a glycolipid 'membrane anchor'. In agreement with… CONTINUE READING

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