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dc.contributor.advisorBabitch, Joseph A.
dc.contributor.authorThompson, Tina Louiseen_US
dc.date.accessioned2019-10-11T15:10:02Z
dc.date.available2019-10-11T15:10:02Z
dc.date.created1986en_US
dc.date.issued1986en_US
dc.identifieraleph-249402en_US
dc.identifier.urihttps://repository.tcu.edu/handle/116099117/31788
dc.description.abstractChick forebrain synaptosomes were incubated with inorganic phosphate (('32)Pi) under conditions which result in the labeling of only internal components. The synaptosomes were rapidly subfractionated into synaptic plasma membranes (SPM), crude synaptic vesicles (SV) synaptoplasm, and mitochondria. Seventeen SPM polypeptides incorporated substantial amounts of ('32)Pi with a 242,000/234,000 dalton doublet displaying greatest incorporation. This polypeptide specifically bound anti-brain spectrin IgG. These data represent an unambiguous discrimination of internally exposed SPM phosphoproteins and demonstrate that the phosphate groups on brain spectrin display rapid turnover in isolated avian nerve endings. p-Chloromercuribenzoic acid (PCMB) was shown to be a potent inhibitor of protein kinases and phosphatases. It is suggested that PCMB will be a useful tool for identifying the role of phosphorylation in neurotransmitter release. Actin, a cytoskeletal compound, is known to have one high affinity cation binding site. Five different cleavage techniques were used to investigate the identify of the calcium binding site on actin. Data suggests that the high affinity binding site is between trp 79 and glu 226. These results together with structural analysis suggest the Ca-binding site is not a classic EF-hand domain.
dc.format.extentxi, 157 leaves, bound : illustrationsen_US
dc.format.mediumFormat: Printen_US
dc.language.isoengen_US
dc.relation.ispartofTexas Christian University dissertationen_US
dc.relation.ispartofAS38.T488en_US
dc.subject.lcshSynaptosomesen_US
dc.subject.lcshPhosphorylationen_US
dc.subject.lcshCalcium-binding proteinsen_US
dc.titleChick brain synaptosomal polypeptides: phosphorylation and calcium binding studiesen_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 .T488 (Regular Loan)
dc.identifier.callnumberSpecial Collections: AS38 .T488 (Non-Circulating)
etd.degree.nameDoctor of Philosophy
etd.degree.grantorTexas Christian University


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