Faculty Advisor

Gelling, R.D. D.

Abstract

Gamma-D Crystallin is a component of the eye lens, but its function is completely unknown. There is little understood about Gamma-D Crystallin due to the difficulty of purifying meaningful quantities in order to perform biochemical assays. The two functions ascribed to crystallins are protein folding and the inhibition of proteases. Therefore, the goal of this project was to develop a better purification method to increase product yield and to determine some of the biochemical properties of Gamma-D Crystallin. Through the use of an Nde I assay and a protein aggregation assay it was determined that Gamma-D is not a general purpose protein folder. Gamma-D was found to exhibit protease inhibitor activity based on a novel enzyme assay that detects protease activity from culture media of Serratia marcescens.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2002

Major

Biotechnology

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Business

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