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Analytical Biochemistry|May 15, 1984
A method for specific chemical modification of gamma-carboxyglutamic acid residues in proteinsS F Wright, C D Bourne, R A Hoke, et al.
International Journal of Peptide and Protein Research|December 1, 1986
Synthesis of a gamma-carboxyglutamic acid containing heptapeptide corresponding to bovine prothrombin residues 17-23R A Hoke, D W Deerfield, L G Pedersen, et al.
The Journal of Biological Chemistry|August 10, 1981
Europium(III) binding to bovine prothrombin residues 1-39 and to bovine prothrombin fragment 1H C Marsh, M M Sarasua, D A Madar, et al.
Biochemical and Biophysical Research Communications|October 15, 1984
Inactivation of human blood coagulation factor X by chemical modification of gamma-carboxyglutamic acid residuesG B Sherrill, D L Straight, R G Hiskey, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 15, 1991
Solution conformations of the gamma-carboxyglutamic acid domain of bovine prothrombin fragment 1, residues 1-65P S Charifson, T Darden, A Tulinsky, et al.
International Journal of Peptide and Protein Research|July 1, 1990
Synthesis and characterization of 1,1,4,4-butanetetracarboxylic acid. A di-gamma-carboxyglutamic acid (GlaGla) analogueS E Cabaniss, K C Pugh, P S Charifson, et al.
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