{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T15:50:48Z","timestamp":1772898648355,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,4,15]]},"abstract":"<jats:p>An Arg-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes (PMNs) was confirmed by the use of diethylamino(benzylidineamino)guanidine (DEA-BAG) as an ADP-ribose acceptor. Two separate HPLC systems were used to separate ADP-ribosyl-DEA-BAG from reaction mixtures, and its presence was confirmed by electrospray mass spectrometry. ADP-ribosyl-DEA-BAG was produced in the presence of PMNs, but not in their absence. Incubation of DEA-BAG with ADP-ribose (0.1\u201310 mM) did not yield ADP-ribosyl-DEA-BAG, which indicates that ADP-ribosyl-DEA-BAG formed in the presence of PMNs was not simply a product of a reaction between DEA-BAG and free ADP-ribose, due possibly to the hydrolysis of NAD+ by an NAD+ glycohydrolase. The assay of mono(ADP-ribosyl)transferase with agmatine as a substrate was modified for intact PMNs, and the activity was found to be approx. 50-fold lower than that in rabbit cardiac membranes. The Km of the enzyme for NAD+ was 100.1\u00b130.4 \u03bcM and the Vmax 1.4\u00b10.2 pmol of ADP-ribosylagmatine\/h per 106 cells. The enzyme is likely to be linked to the cell surface via a glycosylphosphatidylinositol anchor, since incubation of intact PMNs with phosphoinositol-specific phospholipase C (PI-PLC) led to a 98% decrease in mono(ADP-ribosyl)transferase activity in the cells. Cell surface proteins were labelled after exposure of intact PMNs to [32P]NAD+. Their molecular masses were 79, 67, 46, 36 and 26 kDa. The time course for labelling was non-linear under these conditions over a period of 4 h. The labelled products were identified as mono(ADP-ribosyl)ated proteins by hydrolysis with snake venom phosphodiesterase to yield 5\u00b4-AMP.<\/jats:p>","DOI":"10.1042\/bj3150635","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:48:38Z","timestamp":1439243318000},"page":"635-641","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes"],"prefix":"10.1042","volume":"315","author":[{"given":"Louise E.","family":"DONNELLY","sequence":"first","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nigel B.","family":"RENDELL","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen","family":"MURRAY","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jennifer R.","family":"ALLPORT","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gar","family":"LO","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Panagiotis","family":"KEFALAS","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Graham W.","family":"TAYLOR","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"MacDERMOT","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology, Royal Postgraduate Medical School, Du Cane Road, London W12 0NN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/315\/2\/635\/619728\/bj3150635.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/315\/2\/635\/619728\/bj3150635.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:12:29Z","timestamp":1637712749000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/315\/2\/635\/32832\/Arginine-specific-mono-ADP-ribosyl-transferase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,4,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1996,4,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3150635","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,4,15]]}}}