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Full-Text Articles in Life Sciences
Sequence Of A Psac Gene From The Cyanobacterium Synechococcus Sp. Pcc 6301, Patricia L. Herman, Kartika Adiwilaga, John H. Golbeck, Donald P. Weeks
Sequence Of A Psac Gene From The Cyanobacterium Synechococcus Sp. Pcc 6301, Patricia L. Herman, Kartika Adiwilaga, John H. Golbeck, Donald P. Weeks
Department of Biochemistry: Faculty Publications
The psaC gene encodes PsaC, the apoprotein for the terminal iron-sulfur clusters, FA and FB, in the PSI reaction center of cyanobacteria, algae, and higher plants. PsaC functions as a membrane-bound oxidoreductase, accepting electrons from the Fx iron-sulfur cluster located on the PsaA/PsaB heterodimer and donating them to the soluble electron transfer proteins Fd and flavodoxin (reviewed in Bryant, 1992). The objective of our work is to clarify the role of PsaC in linear and cyclic electron transfer. The experimental organism is Syneckococcus sp. PCC 6301, a unicellular, freshwater cyanobacterium that is used extensively for physiological, …
Characteristics Of Modified Leghemoglobins Lsolated From Soybean (Glycine Max Merr.) Root Nodules, Hyung-Kyun Jun, Gautam Sarath, Jose F. Moran, Manuel Becana, Robert V. Klucas, Fred W. Wagner
Characteristics Of Modified Leghemoglobins Lsolated From Soybean (Glycine Max Merr.) Root Nodules, Hyung-Kyun Jun, Gautam Sarath, Jose F. Moran, Manuel Becana, Robert V. Klucas, Fred W. Wagner
Department of Biochemistry: Faculty Publications
Hemoprotein derivatives of an abundant soybean (Glycine max Merr.) root nodule leghemoglobin, Lba, were studied for their modified spectral characteristics and physical properties. Three modified hemoprotein derivatives of Lba (Lbam1, Lbam2, and Lbam3) were purified by preparative isoelectric focusing. The ferric forms of these pigments were green and exhibited anomalous spedra in the visible region as compared to the Lba3+ forms. These modified pigments showed a hypochromic shift of 10 nm for the charge transfer absorption maximum; however, differences were not apparent in the Sdret region. Upon binding with nicotinate, the α …
Exopeptidase Catalyzed Site-Specific Bonding Of Supports, Labels And Bioactive Agents To Proteins, Fred W. Wagner, Thomas R. Coolidge, Dwane E. Wylie, Sheldon M. Schuster, William Lewis, Jay Stout
Exopeptidase Catalyzed Site-Specific Bonding Of Supports, Labels And Bioactive Agents To Proteins, Fred W. Wagner, Thomas R. Coolidge, Dwane E. Wylie, Sheldon M. Schuster, William Lewis, Jay Stout
Department of Biochemistry: Faculty Publications
The invention provides a means for attaching a label, support or bioactive agent to a protein with an exopeptidase at a site that is remote from the active site of the protein. More specifically the invention is directed to a method for the attachment of an amino acid, amine and alcohol nucleophile to the carboxyl terminus of a protein. In one embodiment, a labeled nucleophile is attached to a protein such as an antibody. In other embodiments, the invention is directed to a method for the attachment of a protein to an immobilization support and to a method for the …