Oxidative capacity of skeletal muscle fibres in racehorses: histochemical versus biochemical analysis. 1988

S Valberg, and B Essén Gustavsson, and H Skoglund Wallberg
Department of Medicine I, Faculty of Veterinary Medicine, Swedish University of Agricultural Sciences, Uppsala, Sweden.

The oxidative capacity of skeletal muscle fibre types was evaluated histochemically using the nicotinamide dinucleotide diaphorase (NADH-D) staining, and biochemically by measuring the activity of citrate synthase (CS) in both whole muscle samples and in pools of fibres of identified type. Duplicate determinations of the NADH-D staining pattern resulted in standard deviations (sd) between duplicates of 6 and 11 per cent for two observers. The NADH-D pattern was found to differ between observers. Duplicate determinations of CS activity in the same fibre pools resulted in an sd value of 2.9 mumol/g/min. Measurements of whole muscle CS activity did not provide information about the distribution of oxidative capacity among fibre types. The NADH-D stain and CS activity in fibre pools both showed that, in general, type I and IIA fibres had a higher oxidative capacity than type IIB fibres. Biochemical techniques also showed, however, that the CS activity in type I and IIA fibres of different horses could vary as much as twofold, whereas the NADH-D rating showed a high intensity staining for most type I and IIA fibres in all horses. Furthermore, type IIB fibres received a lower NADH-D rating than the other fibre types even when the CS activities were quite similar. For purposes of research, biochemical measurement of oxidative capacity in individual muscle fibre types provides valuable quantitative and comparative information. The ease of histochemical NADH-D staining in comparison to fibre dissections makes this technique more practical for routine estimates of the distribution of oxidative capacity among muscle fibres.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D007652 Oxo-Acid-Lyases Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3. Ketoacid-Lyases,Ketoacid Lyases,Oxo Acid Lyases
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009245 NADH Dehydrogenase A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1. NADH Cytochrome c Reductase,Diaphorase (NADH Dehydrogenase),NADH (Acceptor) Oxidoreductase,NADH Cytochrome c Oxidoreductase,Dehydrogenase, NADH
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D002950 Citrate (si)-Synthase Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7. Citrate Synthase,Synthase, Citrate
D003579 Cytochrome Reductases Reductases, Cytochrome
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
D006736 Horses Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest. Equus caballus,Equus przewalskii,Horse, Domestic,Domestic Horse,Domestic Horses,Horse,Horses, Domestic
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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