Purification of N-Acetylgalactosaminidase by Isoelectric Focusing.
Abstract
An enzyme which converts type A and type B substances to type O is being purified from human placenta as a reagent for preparing type O, universal donor, red blood cells. The enzyme has been purified 820 fold using ammonium sulfate fractionation, isoelectric precipitation of impurities, ethanol fractionation and chromatography. The crude enzyme is in part complexed to a thermolabile inhibitor. The enzyme is unusually stable to heat and has a pH optimum near pH4.6 using p-nitrophenyl-2-acetamido-2 deoxy-alpha-D-galactopyranoside as substrate. Collaborative studies with Dr. David Aminoff of the University of Michigan have shown that the enzyme removed the terminal N-acetylgalactosamine from A substance and the terminal galactose from B substance to form O substance. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 20, 1980
- Accession Number
- ADA092576
Entities
People
- Ray K. Brown
Organizations
- Wayne State University