{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T23:13:51Z","timestamp":1771629231677,"version":"3.50.1"},"reference-count":27,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2004,10,7]],"date-time":"2004-10-07T00:00:00Z","timestamp":1097107200000},"content-version":"vor","delay-in-days":9776,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Annals of Neurology"],"published-print":{"date-parts":[[1978,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>To understand the apparently paradoxical appearance of phosphorylase in muscle cultured from patients with McArdle disease, the enzyme in muscle culture was studied immunologically and electrophoretically. Antibody against normal human muscle phosphorylase completely inhibited the enzyme activity of adult muscle, but it had no effect on phosphorylase activity of muscle cultures from normal individuals or patients with McArdle disease. Also, amounts of antibody that would completely inhibit phosphorylase in mature muscle left about 30% of the activity in muscle obtained from human fetus at four months' gestation.<\/jats:p><jats:p>Acrylamide\u2010disc and slab\u2010gel electrophoresis showed a single band of phosphorylase activity in adult muscle and two bands in fetal muscle. This suggested that at four months' gestation, both fetal and mature forms are present but that only the mature isoenzyme is inhibited by the antibody. The enzyme from cultured muscle gave only a single band, with the electrophoretic mobility of the fetal isoenzyme. These data suggest that phosphorylase activity in muscle cultured from patients with McArdle disease is due to a fetal isoenzyme whose genetic control is different from that of the mature enzyme.<\/jats:p>","DOI":"10.1002\/ana.410030109","type":"journal-article","created":{"date-parts":[[2004,12,31]],"date-time":"2004-12-31T22:53:10Z","timestamp":1104533590000},"page":"60-66","source":"Crossref","is-referenced-by-count":62,"title":["McArdle disease: The mystery of reappearing phosphorylase activity in muscle culture\u2014A fetal isoenzyme"],"prefix":"10.1002","volume":"3","author":[{"given":"Salvatore","family":"Dimauro","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Susan","family":"Arnold","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Armand","family":"Miranda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lewis P.","family":"Rowland","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,10,7]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM197603112941102"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM197211232872128"},{"key":"e_1_2_1_4_2","first-page":"179","article-title":"Heterozygotes in muscle phosphorylase deficiency","volume":"97","author":"Bank WJ","year":"1973","journal-title":"Trans Am Neurol Assoc"},{"key":"e_1_2_1_5_2","first-page":"292","volume-title":"Histochemistry","author":"Barka T","year":"1963"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.72.12.4999"},{"key":"e_1_2_1_7_2","doi-asserted-by":"crossref","first-page":"4824","DOI":"10.1016\/S0021-9258(18)99530-X","article-title":"Interrelationships among glycogen phosphorylase isozymes","volume":"242","author":"Davis CH","year":"1967","journal-title":"J Biol Chem"},{"key":"e_1_2_1_8_2","series-title":"Recent Advances in Myology","first-page":"344","volume-title":"Studies of myogenesis in vitro: I. Changes of creatine kinase, phosphorylase and phosphofructokinase isozymes; II. 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