McGwire, GB and Tan, FL and Michel, B and Rehli, M and Skidgel, RA (1997) Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck GP180, a hepatitis B virus-binding protein. LIFE SCIENCES, 60 (10). pp. 715-724. ISSN 0024-3205,
Full text not available from this repository.Abstract
A unique membrane-bound carboxypeptidase was discovered and characterized in membrane fractions of human skin fibroblasts and the mouse monocyte-macrophage cell line J774A. 1 and was partially purified from human placenta. Enzymatic characterization identified it as a new member of the regulatory B-type metallocarboxypeptidases, different from carboxypeptidases B, E, M, N and U. It is, however, similar to the newly described bovine carboxypeptidase D, suggested to be a homolog of duck gp180, a 180 kDa hepatitis B virus-binding protein. To prove this, a partial cDNA encoding a 20 kDa fragment of the human homolog of duck gp180 was expressed in bacteria and the recombinant protein was purified. Antibodies raised to the protein immunoprecipitated 94% or 72% of the low pH carboxypeptidase activity in human skin fibroblasts or J774A. 1 cells and gave a 175 kDa protein band in Western blots. Thus, carboxypeptidase D is the mammalian homolog of duck gp180 and is distributed in a variety of different cell types.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PURIFICATION; PITUITARY; BRAIN; carboxypeptidases; membrane-bound carboxypeptidase; peptide metabolism; peptide hormone processing; hepatitis B virus-binding protein |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:32 |
| URI: | https://pred.uni-regensburg.de/id/eprint/51093 |
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