Thesis (Ph. D.)--University of Chicago, Dept. of Organismal Biology and Anatomy, March 1997. / Includes bibliographical references. Also available on the Internet.

Thesis (M. Med. Sc.)--University of Hong Kong, 2006.

Thesis (Ph. D.)--Washington State University, August 2007. / Includes bibliographical references.

Calcium/phospholipid-dependent protein kinase (PKC) was purified from P1798 lymphosarcoma. It was demonstrated that uncomplexed calcium and uncomplexed phosphatidylserine are the activators, that the activation of PKC requires that calcium bind first, that the activation of PKC requires that calcium bind first, that high calcium concentrations inhibit PKC activation, and that calcium inhibition can be overcome by phosphatidylserine.

Nonmuscle myosin from bovine thymus was purified, characterized , and phosphorylated with MLCK, H4PK, and Protein Kinase C. Phosphorylation occured exclusively on the myosin regulatory light chain. Phosphorylation by MLCK and H4PK resulted in the activation of the MgATPase activity as well as filament assembly of nonmuscle myosin.

Calcium/calmodulin-dependent protein kinase II (CaM kinase II) is demonstrated to exist in the ß-cell and immunopecipitation. Glucose and potassium significantly stimulate the rapid autophosphorylation of CaM kinase II and proportionally induce autonomous activity of the kinase in a dose-dependent manner that parallels insulin secretion. The activation of CaM kinase II, alloxan, KN-62 and KN-93, suggest that the enzyme is an integral component of insulin secretion and/or related processes in the β-cell.

No description available.

Purified S6/H4 kinase (Mr 60,000) requires autophosphorylation for activation. A rabbit anti-S6/H4 kinase peptide (SVIDPVPAPVGDSHVDGAAK) antibody recognized both the S6/H4 kinase holoenzyme and catalytic domain. Immunoreactivity with p60 kinase protein, and S6/H4 kinase activity were precisely correlated in fractions obtained from ion exchange chromatography of P1798 lymphosarcoma extracts. An enzyme which catalyzed the MgATP-dependent phosphorylation and activation of S6/H4 kinase coeluted with immunoreactivity from Mono 5, but not Mono Q chromatography. Since S6/H4 kinase is homologous with rac-activated PAK65, the observation that phosphorylation is also required for activation suggests a complex mechanism for in vivo activation of the S6/H4 kinase.

Thesis (Ph. D.)--University of Washington, 1998. / Vita. Includes bibliographical references (leaves [76]-87).

Thesis (Ph. D.)--University of Washington, 1996. / Vita. Includes bibliographical references (leaves [68]-80).