Advertisement

The use of glycogen as a substrate for the determination of serum amylase

      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      A modified glycogen procedure has been presented for the determination of serum β-amylase activity. The method uses a stable glycogen buffered substrate, and the amount of amyloclastic activity can be determined by the use of any of several methods for the determination of glucose or total reducing substance. The procedure is simple, rapid, and accurate.
      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Translational Research
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect

      References

        • Sobel H.
        • Myers V.M.
        A Simplified Method for the Determination of Amylase Activity in Serum and Urine Using Glycogen and the Anthrone Reagent.
        J. Lab. & Clin. Med. 1953; 41: 655-659
        • Dreywood R.
        Qualitative Test for Carbohydrate Material.
        in: Anal. Ed. Ind. & Eng. Chem. 18. 1946: 499
        • Friedman H.S.
        A Modification of the Determination of Urea by the Diacetyl Monoxime Method.
        Anal. Chem. 1953; 23: 622-623
        • Somogyi M.
        A New Reagent for the Determination of Sugar.
        J. Biol. Chem. 1945; 160: 61-68
        • Nelson N.
        A Photometric Adaptation of the Somogyi Method for the Determination of Glucose.
        J. Biol. Chem. 1944; 153: 375-381
        • Andersch M.A.
        The Determination of Serum Amylase, With Particular Reference to the Use of Beta-Amylase as the Substrate.
        J. Biol. Chem. 1946; 166: 705-711
        • Myrbäck K.
        ed. 3. The Enzymes. vol. I. Academic Press, 1950: 654-717 (pt. 1)