Date of Award
8-1972
Document Type
Thesis
Degree Name
Doctor of Philosophy (PhD)
Department
Medical
First Advisor
Alan H. Mehler
Abstract
This dissertation deals with several aspects of the structure and catalytic functions of the enzyme fructose - 1,6-diphosphate aldolase (I.U.B. Number 4.1.2.13) isolated from rabbit muscle.
First, it concerns the chemical nature of the proteolytic modifications of aldolase by a-chymotrypsin and subtilopeptidase B (Novo) in producing an enzyme with catalytic properties like those of the aldolase modified by carboxypeptidase A. The a-chymotrypsin modification has been published (C.F. Midelfort and A.H. Mehler, J. Biol. Chem. 247. 3127 (1972)).
Second it presents evidence for the occurrence of a slow deamidation of an asparagine residue in muscle aldolase in vivo which results in the appearance of electrophoretic isozymes. The results of this study have also been published (Proc. Nat. Acad. Sc i ., U.S. 72, 1935 (1972)).
Third it presents the results of a study designed to compare the binding properties of native and carboxypeptidase A modified aldolases for diphosphate substrate analogues of varying chain lengths.