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Virginia Polytechnic Institute and State University

Factors affecting the activity and stability of aspartate transcarbamylase from Chlorella

Abstract

dc:description.abstract

Aspartate transcarbamylase (carbamoyl phosphate: Laspartate carbamoyltransferase, E.C. 2.1.3.2.) activity from a thermophilic strain 7-11-05 of Chlorella pyrenoidosa appears to be stabilized during and after (NH₄)₂SO₄ precipitation of the enzyme by at least two factors, one having a molecular weight greater than 10,000 and the other having a molecular weight less than 10,000. The high molecular weight factor(s) appears to be an albumin-like protein which is important in stabilizing the activity of the reconstituted enzyme during storage in buffer. The low molecular weight factor(s) is necessary for stabilization of enzyme activity both during and after (NH₄)₂SO₄ precipitation, and it appears to be organic in nature. Stabilization of enzyme activity in whole son1cates during aging appears to be dependent on a heat-stable factor(s) which has a molecular weight of less than 1,000. Aspartate transcarbamylase activity can be stabilized and modulated in vitro by a number of different compounds such as carbamoyl phosphate, UMP, uridine, and cytidine. This low molecular weight stabilizing factor(s) is suggested to be similar to the low molecular weight factor(s) necessary for stabilization of the enzyme during and after (NH₄)₂SO₄ precipitation. The decay of enzyme activity during aging in vitro is proposed to be due to a breakdown of a polymeric form of aspartate transcarbamylase into subunits which have greater catalytic activity than the native enzyme and which are labile 1n the absence of a stabilizing factor(s). An active breakdown of a stabilizing factor(s) could not be observed in whole sonicates, and proof of an active breakdown of the enzyme itself must await further experimentation.

Degree

thesis:*
Name thesis:degree_name
Master of Science
Level thesis:degree_level
masters
Discipline thesis:degree_discipline
Biochemistry and Nutrition
Department dc:contributor.department
Biochemistry and Nutrition
Grantor dc:publisher
Virginia Polytechnic Institute and State University
Year dc:date.issued
1970

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Weeks, James Graham

Rights

dc:rights
Statement dc:rights
  • In Copyright
Language dc:language.iso
en

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/10919/76131
OAI identifier oai:identifier
oai:vtechworks.lib.vt.edu:10919/76131

Chain of custody

source
Harvested from
Virginia Tech
Base URL
vtechworks.lib.vt.edu/oai/request
Last updated
2026-07-22
Source record
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related terms
citation

Weeks, James Graham. Factors affecting the activity and stability of aspartate transcarbamylase from Chlorella. masters thesis, Virginia Polytechnic Institute and State University, 1970. http://hdl.handle.net/10919/76131