NAD: Guanidino group specific mono ADP-ribosyltransferase activity in skeletal muscle

Gopalan Soman, James R. Mickelson, Charles F. Louis, Donald J. Graves

Research output: Contribution to journalArticlepeer-review

61 Scopus citations

Abstract

The sarcoplasmic reticulum and glycogen pellet derived from rabbit skeletal muscle and the sarcolemma and sarcoplasmic reticulum from pig skeletal muscle contains NAD:dependent mono ADP-ribosyltransferase activity toward the guanidine analog, P-nitrobenzylidine aminoguanidine. No or little activity could be found in the sarcolemma or sarcoplasmic reticulum derived from canine cardiac muscle. Seventy percent of activity extracted from rabbit skeletal muscle is localized in the sarcoplasmic reticulum. The enzyme has a pH optimum of 7.4, and KM of 0.5 mM and 0.35 mM for NAD and p-nitrobenzylidine aminoguanidine, respectively. Inorganic phosphate, KCl, and guanidine derivatives inhibit the reaction. Incubation of the sarcoplasmic reticulum or glycogen pellet with (adenylate-32P) NAD or [adenosine-14C(U)]-labeled NAD results in the incorporation of radioactivity into proteins. A large number of proteins are labeled in the sarcoplasmic reticulum fraction. The major labeled band in the glycogen pellet corresponds to a protein of molecular weight of 83 K.

Original languageEnglish (US)
Pages (from-to)973-980
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume120
Issue number3
DOIs
StatePublished - May 16 1984

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