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Kinetic Characterization of Caenorhabditis elegans postembryonic Glyceraldehyde-3-Phosphate Dehydrogenase

Permanent Link: http://ncf.sobek.ufl.edu/NCFE004865/00001

Material Information

Title: Kinetic Characterization of Caenorhabditis elegans postembryonic Glyceraldehyde-3-Phosphate Dehydrogenase
Physical Description: Book
Language: English
Creator: Silimon, Ruth
Publisher: New College of Florida
Place of Publication: Sarasota, Fla.
Creation Date: 2013
Publication Date: 2013

Subjects

Subjects / Keywords: Kinetics
C. Elegans
Glyceraldehyde-3-Phosphate Dehydrogenase
Genre: bibliography   ( marcgt )
theses   ( marcgt )
government publication (state, provincial, terriorial, dependent)   ( marcgt )
born-digital   ( sobekcm )
Electronic Thesis or Dissertation

Notes

Abstract: Caenorhabditis elegans is a model organism in modern biological research. The worm has four different genes, gpd 1-4, for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). GAPDH catalyzes the oxidation and phosphorylation of glyceraldehyde-3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG) using NAD+ and Pi as substrates. The 1,3-BPG product is used in a later reaction in glycolysis to generate ATP. The physiological significance of multiple GAPDH isoenzymes within C. elegans is still not understood. This is the first project to characterize partially purified GPD-3 formally. The IMPACT purification system from NEB was used in conjunction with Rosetta (DE3) cell hosts to over-express and partially purify the enzyme. Enzyme kinetics were performed with all three substrates at pH 8.0. The Km values for NAD+, G3P, and Pi were estimated to be 0.3 mM, 2.6 mM, and 0.4 mM, respectively. The enzyme's specific activity was found to be within the range of 3.6 to 5.3 µmol/min•mg. The Km for NAD+ reported here is lower than the value found for an endogenous GPD mixture however, the Km for G3P is much higher, suggesting the need for further analysis.
Statement of Responsibility: by Ruth Silimon
Thesis: Thesis (B.A.) -- New College of Florida, 2013
General Note: Online version not currently available.
Electronic Access: RESTRICTED TO NCF STUDENTS, STAFF, FACULTY, AND ON-CAMPUS USE
Bibliography: Includes bibliographical references.
Source of Description: This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida Libraries, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.
Local: Faculty Sponsor: Walstrom, Katherine

Record Information

Source Institution: New College of Florida
Holding Location: New College of Florida
Rights Management: Applicable rights reserved.
Classification: local - S.T. 2013 S58
System ID: NCFE004865:00001

Permanent Link: http://ncf.sobek.ufl.edu/NCFE004865/00001

Material Information

Title: Kinetic Characterization of Caenorhabditis elegans postembryonic Glyceraldehyde-3-Phosphate Dehydrogenase
Physical Description: Book
Language: English
Creator: Silimon, Ruth
Publisher: New College of Florida
Place of Publication: Sarasota, Fla.
Creation Date: 2013
Publication Date: 2013

Subjects

Subjects / Keywords: Kinetics
C. Elegans
Glyceraldehyde-3-Phosphate Dehydrogenase
Genre: bibliography   ( marcgt )
theses   ( marcgt )
government publication (state, provincial, terriorial, dependent)   ( marcgt )
born-digital   ( sobekcm )
Electronic Thesis or Dissertation

Notes

Abstract: Caenorhabditis elegans is a model organism in modern biological research. The worm has four different genes, gpd 1-4, for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). GAPDH catalyzes the oxidation and phosphorylation of glyceraldehyde-3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG) using NAD+ and Pi as substrates. The 1,3-BPG product is used in a later reaction in glycolysis to generate ATP. The physiological significance of multiple GAPDH isoenzymes within C. elegans is still not understood. This is the first project to characterize partially purified GPD-3 formally. The IMPACT purification system from NEB was used in conjunction with Rosetta (DE3) cell hosts to over-express and partially purify the enzyme. Enzyme kinetics were performed with all three substrates at pH 8.0. The Km values for NAD+, G3P, and Pi were estimated to be 0.3 mM, 2.6 mM, and 0.4 mM, respectively. The enzyme's specific activity was found to be within the range of 3.6 to 5.3 µmol/min•mg. The Km for NAD+ reported here is lower than the value found for an endogenous GPD mixture however, the Km for G3P is much higher, suggesting the need for further analysis.
Statement of Responsibility: by Ruth Silimon
Thesis: Thesis (B.A.) -- New College of Florida, 2013
General Note: Online version not currently available.
Electronic Access: RESTRICTED TO NCF STUDENTS, STAFF, FACULTY, AND ON-CAMPUS USE
Bibliography: Includes bibliographical references.
Source of Description: This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida Libraries, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.
Local: Faculty Sponsor: Walstrom, Katherine

Record Information

Source Institution: New College of Florida
Holding Location: New College of Florida
Rights Management: Applicable rights reserved.
Classification: local - S.T. 2013 S58
System ID: NCFE004865:00001

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