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  • Book
    edited by Alexander L. Eastman, David H. Rosenbaum, Erwin R. Thal.
    Digital Access ScienceDirect c2009
    Print Access Request
    Location
    Version
    Call Number
    Items
    Books: General Collection (Downstairs)
    2009
    RD93 .P3 2009
    1
  • Article
    Soyama K, Ono E, Shimada N, Tanaka K, Oya N.
    Clin Chim Acta. 1977 Aug 01;78(3):473-8.
    The physico-chemical and electrophoretical properties of alpha-glucosidases from various human tissues and urine have been studied. There were some differences among Peak I enzymes (neutral alpha-glucosidases) obtained from liver, heart, muscle, kidney and urine. These differences are based on different effects of tris(hydroxymethyl)aminomethane and various thermostabilities of the Peak I enzymes. Electrophoretically, the Peak I enzyme activity at pH 6.5 from control tissues displayed a two-banded pattern except in kidney and urine. In the patient with the adult form of Pompe's disease the faster band of the Peak I enzyme from heart and muscle was not found and the slower band of the Peak I enzyme from liver was more cathodic. The results are discussed in relation to glycogenosis type II (Pompe's disease).
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