Amine-specificity of the inactivating ornithine decarboxylase modification in Physarum polycephalum
نویسندگان
چکیده
منابع مشابه
Purification and properties of ornithine decarboxylase from Physarum polycephalum.
Ornithine decarboxylase (EC 4.1.1.17) has been purified 3,500-fold from the plasmodia of Physarum polycephalum. The purified material exhibited a Km for ornithine of 0.6 mM and Vmax of 20 mumol of CO2 formed per min/mg at 30 degrees C (62 mumol/min/mg at 37 degrees C). It migrated as a single protein and activity species on high pressure liquid chromatography (TSK-3000) in 0.15 M NaCl (Mr = 80,...
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The molecular mechanism for polyamine-stimulated feedback modification of ornithine decarboxylase isolated from Physarum polycephalum was investigated by using two-dimensional polyacrylamide-gel electrophoresis. Partially purified A-form enzyme was converted into the B-form enzyme by isolated fractions of the Physarum A-B-converting protein, and the substrates and products were subsequently lab...
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In the paper we proposed a novel model of unconventional computing where a structural part of computation is presented by dynamics of Plasmodium of Physarum polycephalum, a large single cell. We sketch a new logical approach combining conventional logic with process calculus to demonstrate how to employ formal methods in design of unconventional computing media presented by Physarum polycephalu...
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Physarumpolycephalum is an acellular slime mould whose histones are of general interest because they allow comparisons to be made between lower eukaryote and higher eukaryote histones and, perhaps more importantly, they provide a unique opportunity for the study of histone changes in the mitotic cycle, which is naturally synchronous in P. polycephalum plasmodia, and during differentiation. Stud...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1982
ISSN: 0264-6021
DOI: 10.1042/bj2050551