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Published on: September 29, 2019
Human mast cell carboxypeptidase. Purification and characterization.
S M Goldstein1, C E Kaempfer, J T Kealey
1Department of Dermatology, University of California, San Francisco 94143.
The Journal of Clinical Investigation
|May 1, 1989
Summary
Human mast cell carboxypeptidase, a novel enzyme, was purified and characterized. It shows functional similarities to carboxypeptidase A but structural similarities to carboxypeptidase B.
Area of Science:
- Biochemistry
- Enzymology
- Cell Biology
Background:
- Carboxypeptidase activity has been identified in human mast cells.
- Mast cells play crucial roles in allergic responses and inflammation.
Purpose of the Study:
- To purify and characterize carboxypeptidase from human mast cells.
- To determine the biochemical and structural properties of human mast cell carboxypeptidase.
Main Methods:
- Purification using affinity chromatography with a potato-tuber carboxypeptidase inhibitor.
- SDS-PAGE for molecular weight determination.
- Enzyme activity assays (hydrolysis of dipeptides and angiotensin I).
- Amino acid composition and N-terminal sequencing.
Main Results:
- Human mast cell carboxypeptidase was purified to homogeneity with a molecular weight of approximately 34,500 D.
- The enzyme exhibited carboxypeptidase A-like activity on synthetic substrates and angiotensin I, but not des-Arg9 bradykinin.
- Amino acid composition was similar to rat mast cell carboxypeptidase.
- N-terminal sequencing showed 65% identity with human pancreatic carboxypeptidase B and 19% with human carboxypeptidase A.
Conclusions:
- Human mast cell carboxypeptidase is a novel zinc-containing carboxypeptidase.
- It is functionally distinct from carboxypeptidase A but structurally related to carboxypeptidase B.
- This enzyme may play a unique role in mast cell-mediated processes.
