Lipid catabolism in Treponema

Members of the genus, Treponema, require long-chain fatty acids for growth in vitro. Serum, added to culture medium, provides a source of long-chain fatty acids. These fatty acids, however, are esterified to triglycerides, phospholipids, and cholesterol. In this study, the major pathways of complex lipid catabolism in five species of Treponema were investigated. Lipase, the enzyme which hydrolyzes triglycerides, was demonstrated using four lipid substrates in five species. Chromatographic data demonstrated that, during growth, treponemes completely utilized lysophosphatidylcholine, present in serum-supplemented culture medium, while phosphatidylcholine and phosphatidylinositol were not utilized. Whole cultures and cell free extracts were examined for the presence of specific enzymes of phospholipid catabolism. Phospholipase B and glycerophosphorylcholine diesterase activities were demonstrated in five species of Treponema. Acid phosphatase activity was demonstrated in two species. Utilization of L-α-glycerophosphate and glycerol, products of phospholipid catabolism, was examined. Glycerol was utilized from culture medium by one species, while α-glycerophosphate was utilized by four species. Phospholipases A, C, and D, α-glycero-phosphate dehydrogenase, and alkaline phosphatase activities were not found in five species of Treponema. Based on the specific enzymes demonstrated in this study, two pathways of phospholipid catabolism are proposed.

Name thesis:degree_name

M.S.

Level thesis:degree_level

masters

Discipline thesis:degree_discipline

Microbiology

Department dc:contributor.department

Microbiology

Grantor dc:publisher

Virginia Polytechnic Institute and State University

Year dc:date.issued

1978

Author dc:creator

• Trevathan, Carol Ann

Statement dc:rights

• In Copyright

Licence dc:rights.uri

• http://rightsstatements.org/vocab/InC/1.0/

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10919/113480

OAI identifier oai:identifier

oai:vtechworks.lib.vt.edu:10919/113480