Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Harry W. Eckerson"'
Publikováno v:
Journal of Biological Chemistry. 254:8324-8330
Highly purified “usual” human serum cholinesterase was studied. The enzyme is a tetramer with a molecular weight of approximately 340,000. Its four subunits appear to be identical. On 1% sodium dodecyl sulfate (SDS) gel electrophoresis the enzyme
Publikováno v:
Cardiovascular Drug Reviews. 3:85-97
Autor:
Ronald L. Menlove, Charles F. Dahl, Gary P. Symkoviak, Jeffrey L. Anderson, Robert L. Rothbard, Sherman G. Sorensen, Arthur D. Hagan, Harry W. Eckerson, Patricia G. Fitzpatrick, Rosemary A. Hackworthy, Kevin F. Browne, Victor J. Marder, William H. Barry
Publikováno v:
Journal of the American College of Cardiology. (6):1153-1163
The recent establishment of a firm therapeutic role for reperfusion in acute myocardial infarction has stimulated interest in the development of more ideal thrombolylic agents. Anisoylated plasminogen streptokinase activator complex (APSAC) is a new
Publikováno v:
Biochemical pharmacology. 30(12)
V max and K m values with twenty-five “atypical” and thirty-seven “usual” cholinesterase human sera were determined for the cholinesterase substrates procaine, tetracaine, benzoylcholine, o -nitro-phenylbutyrate, α-naphthylacetate and aspiri