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Original

Glycogen Phosphorylase Activity in Biopsy Samples and Single Muscle Fibres of Musculus Quadriceps Femoris of Man at Rest

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Pages 521-526 | Received 09 Feb 1976, Accepted 09 Apr 1976, Published online: 14 Feb 2011
 

Abstract

Harris, R. C, Essén, B. & Hultman, E. Glycogen Phosphorylase Activity in Biopsy Samples and Single Muscle Fibres of Musculus Quadriceps Femoris of Man at Rest. Scand. J. clin. Lab. Invest. 36, 521–526, 1976.

Glycogen phosphorylase activity in biopsy samples of the quadriceps muscle of man taken at rest was measured in the direction of glycogen breakdown. The conditions of assay used were pH 6.8 and 35 d`C. Mean phosphorylase activity per kg fresh muscle in 8 male volunteers was: phosphorylase a - 259 U, and total phosphorylase - 627 U, where 1U is the production of 1 μmol glucose-1-phosphate/s under the conditions of assay. The mean value of total activity, transposed to the in vivo condition, is sufficient to support a maximum rate of glycogen degradation calculated as glucosyl units utilized per kg fresh muscle, of 627 μmol/s. This is approximately the rate at which glycolysis occurs during a maximum voluntary isometric contraction. The mean ratio of phosphorylase a activity to total activity at rest was 0.40. Estimates of the mean total phosphorylase activity in type I (‘slow’) muscle fibres isolated from the quadriceps of 9 volunteers ranged from 210–385 U/kg fresh muscle, and in type II (‘fast’) muscle fibres from 493–934 U/kg fresh muscle. The average ratio of activity in type II fibres compared with that in type I fibres was 2.5.

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