Biochemical Characterization of Matrix Gla Protein - Villa, Francisco
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The purpose of this dissertation was: 1) to biochemically characterize how purified matrix Gla protein (MGP) functions as a calcification inhibitor using two novel in vitro calcification assays; 2) to characterize MGP s binding to apatite mineral; and 3) to characterize MGP purified from bone, cartilage, and serum using mass spectrometry. The data presented in this dissertation provide for the first time evidence of how purified MGP acts as an inhibitor of calcification and establishes that MGP accomplishes this function through direct interaction with calcium phosphate mineral.

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Produktbeschreibung
The purpose of this dissertation was: 1) to biochemically characterize how purified matrix Gla protein (MGP) functions as a calcification inhibitor using two novel in vitro calcification assays; 2) to characterize MGP s binding to apatite mineral; and 3) to characterize MGP purified from bone, cartilage, and serum using mass spectrometry. The data presented in this dissertation provide for the first time evidence of how purified MGP acts as an inhibitor of calcification and establishes that MGP accomplishes this function through direct interaction with calcium phosphate mineral.
Autorenporträt
Francisco, originally from Southern Arizona, completed this work while at the University of California, San Diego in the Department of Chemistry and Biochemistry. His interests involve chemical and biological education at the college level and research understanding the biochemistry of bone matrix associated proteins.