Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types

Am J Anat. 1981 Feb;160(2):175-86. doi: 10.1002/aja.1001600204.


The profiles of fiber types in hindlimb muscles from the tree shrew (Tupaia glis), lesser bushbaby (Galago senegalensis), and the slow loris (Nycticebus coucang) were determined using histochemical techniques. Fibers were classified as fast-twitch oxidative-glycolytic (FOG), fast-twitch glycolytic (FG), slow-twitch oxidative (SO), or fast-twitch oxidative (FO), according to reactions for alkaline-stable ATPase, acid-stable ATPase, alpha-glucan phosphorylase, reduced nicotinamide adenine dinucleotide diaphorase, succinate dehydrogenase, mitochondrial alpha-glycerophosphate dehydrogenase (MaGPDH), and beta-hydroxybutyric dehydrogenase, as well as glycogen staining by the periodic acid-Schiff technique. Prolonged dissection of numerous muscles was carried out on hindlimbs submersed in cold Tyrode's solution; such treatment had no qualitative effect on enzyme staining reactions, but it is not a suitable procedure if one wishes to stain for glycogen. Fast-twitch oxidative (FO) fibers are alkaline-stable ATPase-positive and possess low MalphaGPDH enzyme activity. These fibers have not been reported previously in any hindlimb muscles. No muscles of any species studies were homogeneous with respect to fiber type. Slow loris muscles lacked FG fibers. The majority of the muscles of the slow loris contained numerous SO fibers. The relationship between enzyme activities and locomotor pattern is discussed.

Publication types

  • Comparative Study

MeSH terms

  • Adenosine Triphosphatases / analysis
  • Animals
  • Female
  • Galago / anatomy & histology
  • Glycogen / analysis
  • Hindlimb / anatomy & histology*
  • Hindlimb / physiology
  • Histocytochemistry
  • Lorisidae / anatomy & histology
  • Male
  • Movement
  • Muscles / enzymology
  • Muscles / physiology*
  • Strepsirhini / anatomy & histology*
  • Tupaiidae / anatomy & histology


  • Glycogen
  • Adenosine Triphosphatases