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dc.contributor.advisorBobich, Joseph A.
dc.contributor.authorAnthony, Francis Andrewen_US
dc.date.accessioned2019-10-11T15:10:02Z
dc.date.available2019-10-11T15:10:02Z
dc.date.created1984en_US
dc.date.issued1984en_US
dc.identifieraleph-236869en_US
dc.identifier.urihttps://repository.tcu.edu/handle/116099117/31785
dc.description.abstractA method was improved to detect ('45)Ca('2+)-binding proteins in polyacrylamide gels. It was shorter, quantitative, highly reproducible, and resulted in a 40-fold enhanced sensitivity over the previous method. The technique could detect proteins in polyacrylamide gels with different modes of Ca('2+) binding and different dissociation constants. It could also detect EF hand containing proteins in polyacrylamide gels in the nanogram range. All major isoforms of actin were observed to bind ('45)Ca('2+). Sequence analysis revealed the presence of an highly conserved region in all actins that contained a variant EF hand. This variant EF hand was probably the calcium-binding site, possibly involved in inhibiting actin nucleation. Both (alpha) and (beta) tubulin were observed to bind ('45)Ca('2+). Sequence analysis revealed the presence of variant EF hands. Like the actins, this variant EF hand was probably the calcium-binding site, possibly involved in inhibition of tubulin nucleation. Proteins from each of the 5 classes of intermediate filaments bound ('45)Ca('2+). Sequence analysis revealed the presence of variant EF hands in the intermediate filament proteins of known sequence: vimentin, desmin, keratin, and glial fibrillary acidic protein. These variant EF hands were probably the calcium-binding sites, suggesting a regulatory function for calcium. Whole brain and synaptic subfractions from chick were examined for ('45)Ca('2+)-binding proteins. To ensure isolation of intact synaptosomes for ('45)Ca('2+) binding, an examination of the ultrastructure of chick synaptosomes was made. They were found to be resistant to lower osmotic pressure suggesting synaptosomal species differences. ('45)Ca('2+) analyses of whole brain subfractions (cerebra, cerebella, nuclei, microsomes, brain cytoplasm, myelin, extrasynaptosomal mitchondria) in polyacrylamide gels revealed several ('45)Ca('2+)-binding proteins. Many previously unreported proteins were observed. Synaptic subfractions (synaptosomes, synaptic vesicles, intrasynaptosomal mitochondria, presynaptic membranes, presynaptic cytoplasm) revealed several ('45)Ca('2+)-binding proteins. The majority of ('45)Ca('2+)-binding proteins were found in the presynaptic cytoplasm. Two-dimensional gel electrophoresis and ('45)Ca('2+) binding of this subfraction revealed 14 proteins other than calmodulin which could be triggers for neurotransmitter release.en_US
dc.format.extentxii, 199 leaves, bound : illustrationsen_US
dc.format.mediumFormat: Printen_US
dc.language.isoengen_US
dc.relation.ispartofTexas Christian University dissertationen_US
dc.relation.ispartofAS38.A67en_US
dc.subject.lcshCalcium-binding proteinsen_US
dc.subject.lcshPolyacrylamide gel electrophoresisen_US
dc.titleStudies on calcium-binding proteinsen_US
dc.typeTexten_US
etd.degree.departmentDepartment of Chemistry
etd.degree.levelDoctoral
local.collegeCollege of Science and Engineering
local.departmentChemistry and Biochemistry
local.academicunitDepartment of Chemistry
dc.type.genreDissertation
local.subjectareaChemistry and Biochemistry
dc.identifier.callnumberMain Stacks: AS38 .A67 (Regular Loan)
dc.identifier.callnumberSpecial Collections: AS38 .A67 (Non-Circulating)
etd.degree.nameDoctor of Philosophy
etd.degree.grantorTexas Christian University


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