Show simple item record

dc.contributor.authorPerin, Ivano.en_US
dc.date.accessioned2009-07-09T17:34:28Z
dc.date.available2009-07-09T17:34:28Z
dc.date.issued1996-07-09T17:34:28Z
dc.identifier.urihttp://hdl.handle.net/10464/1805
dc.description.abstractStudies on the steady state behavior of soluble cytochrome c oxidase are extensive. These studies have examined the influence of ionic strength and pH and may provide answers to questions such as the link between proton translocation and charge separation. The present study examined the influence of external bulk pH on ApH formation, biphasic kinetics, and steady state reduction of cytochromes c and a of cytochrome c oxidase in proteoliposomes. Bulk pH has an appreciable effect on ApH formation and steady state reduction levels of cytochromes c and 8. Bulk pH affected total Vmax and Km at the low affinity binding site of cytochrome c. This study also examined the influence of bovine serum albumin and free fatty acids on proton pumping activity in bovine heart proteoliposomes. Proton pumping activity decreased after treatment with BSA, and was subsequently reinstated after further treatment with FFA. Much study in the superfamily of haem/copper oxidases has recently been devoted to the bacterial oxidases. The present study has examined some protein composition characteristics and bioenergetic features of Bacillus subtilis cytochrome caa3 oxidase. Results provide evidence for the structural composition of the enzyme in relation to the covalently bound cytochrome c to the oxidas~. Bioenergetically, caa3 COV showed appreciable proton pumping activity. Steady state analysis of the caa3 COV showed significantly different cytochrome c and a reduction characteristics compared to the bovine enzyme.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectCytochrome c.en_US
dc.subjectCytochrome oxidase.en_US
dc.subjectHeart--Cytopathology.en_US
dc.subjectCattle--Cardiovascular system.en_US
dc.titleComparative study of bovine heart and bacillus subtilis cytochrome c oxidase vesicles and the influence of bulk pH on cytochrome c oxidase componentsen_US
dc.typeElectronic Thesis or Dissertationen_US
dc.degree.nameM.Sc. Biological Sciencesen_US
dc.degree.levelMastersen_US
dc.contributor.departmentDepartment of Biological Sciencesen_US
dc.degree.disciplineFaculty of Mathematics and Scienceen_US
refterms.dateFOA2021-08-07T02:00:13Z


Files in this item

Thumbnail
Name:
Brock_Perin_Ivano_1996.pdf
Size:
12.91Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record