Zobrazeno 1 - 10
of 16
pro vyhledávání: '"G. F. Seelig"'
Autor:
S. Shane Taremi, Birendra N. Pramanik, Xuedon Fan, R. A. O'donnell, Anthony Tsarbopoulos, Hung V. Le, N. Rajan, G. F. Seelig, Samuel Baldwin, Ramasamy Kumarasamy
Publikováno v:
Biochemical and Biophysical Research Communications. 206:694-702
Interleukin 4 (IL-4) mediates its biological activities through interaction with its receptor on the cell surface. A recombinant extracellular domain of the alpha subunit of human interleukin 4 receptor was expressed in CHO cells and purified to homo
Publikováno v:
The Journal of biological chemistry. 269(8)
A synthetic segment (110-127) of the carboxyl terminus of recombinant human granulocyte-macrophage colony-stimulating factor (rh-GM-CSF) was used to generate a rabbit polyclonal antibody (345-6), which recognized both peptide and full-length Escheric
Publikováno v:
The Journal of biological chemistry. 269(1)
The epitopes of two neutralizing antibodies (47N3-6 and 47N30A35) raised against rhuIFN-gamma each mapped both to amino-terminal regions (22-29 and 12-19, respectively) and to a carboxyl-terminal region 131-139, suggesting the juxtaposition of these
Autor:
Y, Kanakura, S A, Cannistra, C B, Brown, M, Nakamura, G F, Seelig, W W, Prosise, J C, Hawkins, K, Kaushansky, J D, Griffin
Publikováno v:
Blood. 77(5)
Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a glycoprotein that is required for the survival, growth, and differentiation of hematopoietic progenitor cells. Although the primary structure of GM-CSF is known from cDNA cloning, the rel
Autor:
G F Seelig, R F Colman
Publikováno v:
Journal of Biological Chemistry. 252:3671-3678
Autor:
R F Colman, G F Seelig
Publikováno v:
Journal of Biological Chemistry. 254:1191-1195
Autor:
J E Folk, G F Seelig
Publikováno v:
Journal of Biological Chemistry. 255:8881-8886
Human blood plasma coagulation factor XIII is a zymogen of subnit structure a2b2. Several modified forms of the isolated noncatalytic b chains from this zymogen have been prepared and tested for their ability to complex noncovalently with preparation
Autor:
G F Seelig, A Meister
Publikováno v:
Journal of Biological Chemistry. 259:3534-3538
gamma-Glutamylcysteine synthetase (isolated from rat kidney) has one sulfhydryl group that reacts with 5,5'-dithiobis-(2-nitrobenzoate). This single exposed sulfhydryl group is not required for enzyme activity. The enzyme is potently inactivated by c
Publikováno v:
The Journal of biological chemistry. 259(15)
gamma-Glutamylcysteine synthetase (rat kidney; Mr approximately 104,000) is composed of 2 nonidentical subunits. In the present work, a procedure was developed for the reversible dissociation of the enzyme into its subunits (Mr = 73,000 and 27,700) u
Autor:
G F, Seelig, R F, Colman
Publikováno v:
The Journal of biological chemistry. 252(11)