Regulation of Adenylate Kinase

While investigating concentration-dependent thermolability in crude homogenates and partially purified preparations of a temperature-sensitive adk mutant of E. coli, a protein was discovered that altered the degree of thermolability of the mutant enzyme. This protein, called an adenylate kinase-associated protein, co-purified with the wild type and mutant enzymes through several purification steps. A homogeneous preparation of the adenylate kinase-associated protein gave a single band on a sodium dodecyl sulfate-polyacrylamide gel with M(,r) = 34,000. The interaction of this protein with adenylate kinase explains why the thermolability of the mutant adenylate kinase changed during purification and the dependence of the thermolability on concentration.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Huss, Ronald John

• Chemistry, Biochemistry

Identifier

(UMI)AAI8600212

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70548