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Mono‐ADP‐Ribosylation in Brain: Purification and Characterization of ADP‐Ribosyltransferases Affecting Actin from Rat Brain
Author(s) -
Matsuyama Satoshi,
Tsuyama Shingo
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08304.x
Subject(s) - synaptosome , nad+ kinase , gel electrophoresis , biology , biochemistry , adp ribosylation , enzyme , nicotinamide , cyclase , guanine , adenylate kinase , transferase , polyacrylamide gel electrophoresis , actin , microbiology and biotechnology , nucleotide , in vitro , gene
Four ADP‐ribosyltransferases that acted on non‐muscle actin were purified more than 3,000‐fold from rat brain extract. The molecular weights of these brain ADP‐ribosyltransferases were 66,000 as estimated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and gel filtration on TSK gel G3000SW. The K m values for NAD were approximately 20 μ M . These enzymes were not inhibited by thymidine or nicotinamide, but were inhibited by ADP and ADP‐ribose. Two soluble ADP‐ribosylation factors purified from rat brain had different effects on the four ADP‐ribosyltransferases during the ADP‐ribosylation of non‐muscle actin. These ADP‐ribosyltransferases modified not only actin but also the stimulatory guanine nucleotide‐binding protein of adenylate cyclase, G s , and another guanine nucleotide‐binding protein in brain, G o . These findings suggest that the four brain ADP‐ribosyltransferases are concerned with nerve functions in the central nervous system.