Zobrazeno 1 - 8
of 8
pro vyhledávání: '"E. D. Eccleston"'
Publikováno v:
Insect molecular biology. 11(2)
An important justification for genome sequencing efforts is the anticipation that data from model organisms will provide a framework for the more rapid analysis of other, less studied genomes. In this investigation, we sequenced an internal region of
Publikováno v:
Nature. 365:496-497
Autor:
E D Eccleston, J B Howard
Publikováno v:
Journal of Biological Chemistry. 260:10169-10176
The human protease inhibitor alpha 2-macroglobulin (alpha 2 M) is inactivated by reaction with methylamine. The site of reaction is a protein functional group having the properties of a thiol ester. To ascertain the relationship between thiol ester c
Publikováno v:
Journal of Biological Chemistry. 254:11399-11404
Histidinol dehydrogenase and UDP-Glc dehydrogenase catalyze 4-electron dehydrogenations that convert primary alcohol groups to the corresponding acids. Both reactions proceed in two distinct steps involving the oxidation of the primary alcohol to a b
Publikováno v:
The Journal of biological chemistry. 254(22)
Histidinol dehydrogenase and UDP-Glc dehydrogenase catalyze 4-electron dehydrogenations that convert primary alcohol groups to the corresponding acids. Both reactions proceed in two distinct steps involving the oxidation of the primary alcohol to a b
Publikováno v:
The Journal of biological chemistry. 264(33)
Monoclonal antibodies have been produced against electrophoretically purified MP18, a major calf lens membrane Mr = 18,000 substrate for cAMP-dependent protein kinase. One of these antibodies (monoclonal antibody 2D10) cross-reacted with both native
Autor:
E D, Eccleston, J B, Howard
Publikováno v:
The Journal of biological chemistry. 260(18)
The human protease inhibitor alpha 2-macroglobulin (alpha 2 M) is inactivated by reaction with methylamine. The site of reaction is a protein functional group having the properties of a thiol ester. To ascertain the relationship between thiol ester c
Publikováno v:
The Journal of biological chemistry. 264(33)
The 18,000-dalton bovine lens fiber cell intrinsic membrane protein MP18 was phosphorylated on a serine residue by both cAMP-dependent protein kinase and protein kinase C. In addition, this protein bound calmodulin and was recognized by a monoclonal