ADP-ribosyltransferase from Helix pomatia. Purification and characterization
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چکیده
منابع مشابه
Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes.
Integral membrane-associated arginine-specific mono-ADP-ribosyltransferase was purified from rabbit skeletal muscle microsomes. The ADP-ribosyltransferase was solubilized from the 100,000 x g pellet with 0.3% sodium deoxycholate and purified to greater than or equal to 95% homogeneity by successive DE52, concanavalin A-agarose, 3-aminobenzamide-agarose, and size-exclusion high-performance liqui...
متن کاملMolecular characterization of a glycosylphosphatidylinositol-linked ADP-ribosyltransferase from lymphocytes.
Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T lymphocytes (CTL) with NAD resulted in the ADP-ribosylation of membrane proteins and inhibition of cell proliferation and cytotoxicity. Treatment of CTL with phosphatidyli...
متن کاملADP-ribosyltransferase from Hen Liver Nuclei
Chromatin-bound ADP-ribosyltransferase from adult hen liver nuclei was purified to a homogeneous state through salt extraction, gel filtration, hydroxyapatite, phenyl-Sepharose, Cm-cellulose, and DNA-Sepharose. The ADP-ribosyltransferase has a pH optimum at 9.0 and does not require DNA for reaction. The purified enzyme has a molecular weight of 27,500 2 500. Agmatine sulfate, arginine methyl es...
متن کاملPartial purification and some properties of a cellulase from Helix pomatia.
The properties of cellulases from Helix pomatia have been studied by many workers, including Seilliere (1906), Karrer, Schubert & Wehrli (1925), Karrer & Schubert (1926, 1928) and de Stevens (1955). Cellulolytic enzymes have also been found in other invertebrates, such as Teredo (Greenfield, 1955) and Ctenolep8ima lineata (Lasker & Giese, 1956), and in a wide range ofmicro-organisms which inclu...
متن کاملPurification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum.
The enzyme that catalyzes the ADP-ribosylation and concomitant inactivation of dinitrogenase reductase in Rhodospirillum rubrum has been purified greater than 19,000-fold to near homogeneity. We propose dinitrogenase reductase ADP-ribosyltransferase (DRAT) as the working name for the enzyme. DRAT activity is stabilized by NaCl and ADP. The enzyme is a monomer with a molecular mass of 30 kDa and...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1987
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2480859