Affiliation:
1. Department of Biology, Biological Research Laboratories, Syracuse University, Syracuse, New York 13210
Abstract
The purification and properties of a tumor inhibitory
l
-asparaginase from
Serratia marcescens
are described. The following properties of the enzyme were examined: kinetics of the enzyme reaction, catalytic activity as a function of
p
H, boundary sedimentation velocity, electrophoresis on polyacrylamide gel, immuno-electrophoresis against homologous and heterologous antisera, immunodiffusion, blood clearance rate in mice, and inhibition of the 6C3HED lymphoma in C3H mice. Complete regression of this tumor was obtained with a smaller dose of the enzyme from
S. marcescens
than with enzyme from
Escherichia coli
. The reason for this difference was not evident from a comparison of several properties of the two enzymes.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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