Zobrazeno 1 - 5
of 5
pro vyhledávání: '"E. B. Nickbarg"'
Autor:
Barry S. Cooperman, E Rescorla, Norman M. Schechter, E. B. Nickbarg, Elena S. Stavridi, Harvey Rubin
Publikováno v:
Journal of Biological Chemistry. 268:23616-23625
The interactions of bovine pancreatic chymotrypsin (Chtr) and recombinant alpha 1-antichymotrypsin (rACT) and rACT variants were studied by kinetic and gel electrophoretic analyses, leading to the formulation of a general kinetic scheme that accounts
Autor:
L Kilpatrick, J L Johnson, E B Nickbarg, Z M Wang, T F Clifford, M Banach, B S Cooperman, S D Douglas, H Rubin
Publikováno v:
The Journal of Immunology. 146:2388-2393
Reactive oxygen intermediates and serine proteases are important components of host defense systems but can produce host injury if not tightly regulated. To determine whether these components can be coordinately controlled, we investigated regulation
Autor:
E. B. Nickbarg, J. L. Johnson, O. L. Schoenberger, Barry S. Cooperman, S. Mclarney, Nirinjini Naidoo, Harvey Rubin, Zhi Mei Wang
Publikováno v:
Journal of Biological Chemistry. 265:1199-1207
Human alpha 1-antichymotrypsin has been cloned, sequenced and expressed in Escherichia coli and recombinant protein as well as point-specific mutants have been purified and characterized. The corrected gene-deduced amino acid sequence has 45% overall
Autor:
L, Kilpatrick, J L, Johnson, E B, Nickbarg, Z M, Wang, T F, Clifford, M, Banach, B S, Cooperman, S D, Douglas, H, Rubin
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 146(7)
Reactive oxygen intermediates and serine proteases are important components of host defense systems but can produce host injury if not tightly regulated. To determine whether these components can be coordinately controlled, we investigated regulation
Autor:
H, Rubin, Z M, Wang, E B, Nickbarg, S, McLarney, N, Naidoo, O L, Schoenberger, J L, Johnson, B S, Cooperman
Publikováno v:
The Journal of biological chemistry. 265(2)
Human alpha 1-antichymotrypsin has been cloned, sequenced and expressed in Escherichia coli and recombinant protein as well as point-specific mutants have been purified and characterized. The corrected gene-deduced amino acid sequence has 45% overall