Student Work

Purification and characterization of gamma-D crystallin

Public

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.

  • This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.
Creator
Publisher
Identifier
  • 02D257M
Advisor
Year
  • 2002
Date created
  • 2002-01-01
Resource type
Major
Rights statement

Relations

In Collection:

Items

Items

Permanent link to this page: https://digital.wpi.edu/show/xd07gx06c