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International Journal of Peptide and Protein Research|May 1, 1983
Studies of the histidine residues of human and bovine glycoprotein hormones by nuclear magnetic resonanceT F Parsons, J G PierceThe Journal of Biological Chemistry|February 25, 1984
Free alpha-like material from bovine pituitaries. Removal of its O-linked oligosaccharide permits combination with lutropin-betaT F Parsons, J G PierceProceedings of the National Academy of Sciences of the United States of America|December 1, 1980
Oligosaccharide moieties of glycoprotein hormones: bovine lutropin resists enzymatic deglycosylation because of terminal O-sulfated N-acetylhexosaminesT F Parsons, J G PierceThe Journal of Biological Chemistry|December 25, 1982
Enzymatic deglycosylation of the subunits of chorionic gonadotropin. Effects on formation of tertiary structure and biological activityJ M Goverman, T F Parsons, J G PierceInternational Journal of Peptide and Protein Research|January 1, 1979
Purification and receptor binding properties of complexes between lutropin and monovalent antibodies against its alpha subunitJ G Pierce, G A Bloomfield, T F ParsonsThe Journal of Biological Chemistry|January 10, 1983
Purification of an alternate form of the alpha subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaccharideT F Parsons, G A Bloomfield, J G PierceEndocrinology|June 1, 1984
Rapid and easy separation of the subunits of bovine and human glycoprotein hormones by use of high performance liquid chromatographyT F Parsons, T W Strickland, J G PierceThe Journal of Biological Chemistry|June 10, 1979
Proton nuclear magnetic resonance studies on bovine lutropin, its subunits, and on the alpha subunit of pregnant mare serum gonadotropin. Assignment of histidine resonances in the alpha subunitF F Brown, T F Parsons, D S Sigman, et al.The Journal of Biological Chemistry|September 10, 1978
Biosynthesis of bacterial glycogen. Incorporation of pyridoxal phosphate into the allosteric activator site and an ADP-glucose-protected pyridoxal phosphate binding site of Escherichia coli B ADP-glucose synthaseT F Parsons, J PreissThe Journal of Biological Chemistry|November 10, 1978
Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthaseT F Parsons, J PreissPageof 4