Poster Title

P-16 The Role of the Prodomain in the Folding of Carboxypeptidase A1

Department

Biology

Abstract

Carboxypeptidase A1 (CPA1) is a digestive enzyme. This enzyme contains a prodomain region, which must be cleaved for enzymatic function. Previous studies have hypothesized that the prodomain is necessary for CPA1 structural stability. However, the discovery of a related enzyme, carboxypeptidase O (CPO), which does not have a prodomain, challenges this assertion. In order to investigate the need for a carboxypeptidase prodomain, or other stabilizing features, an antibody tag was added through polymerase chain reaction (PCR). The prodomain was then removed via PCR. Western Blots and enzyme assays confirmed formation of the protein with the antibody tag and will be performed to determine proper formation and function of CPA1 without the prodomain.

Acknowledgments

Advisor: Peter Lyons, Biology

Location

Buller Hall 208

Start Date

3-11-2022 1:30 PM

End Date

3-11-2022 3:30 PM

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Mar 11th, 1:30 PM Mar 11th, 3:30 PM

P-16 The Role of the Prodomain in the Folding of Carboxypeptidase A1

Buller Hall 208

Carboxypeptidase A1 (CPA1) is a digestive enzyme. This enzyme contains a prodomain region, which must be cleaved for enzymatic function. Previous studies have hypothesized that the prodomain is necessary for CPA1 structural stability. However, the discovery of a related enzyme, carboxypeptidase O (CPO), which does not have a prodomain, challenges this assertion. In order to investigate the need for a carboxypeptidase prodomain, or other stabilizing features, an antibody tag was added through polymerase chain reaction (PCR). The prodomain was then removed via PCR. Western Blots and enzyme assays confirmed formation of the protein with the antibody tag and will be performed to determine proper formation and function of CPA1 without the prodomain.