Myoglobin content and enzymatic activity of human skeletal muscle--their relation with the process of adaptation to high altitude.

Abstract

Abstract : Quantitative determinations of myoglobin were made in the sartorius muscle of healthy human subjects, native of sea-level and high-altitude areas. The specific activity of the reduced form of diphosphopyridine nucleotide oxidase (DPNH-oxidase), DPNH- and TPNH-cytochrome C reductases, transhydrogenase, and isocitric and lactic dehydrogenases were also examined. A significantly higher myoglobin concentration was found in the muscle of the high-altitude natives as compared with sea-level residents. The enzyme systems DPNH-oxidase, TPNH-cytochrome C reductase, and transhydrogenase similarly showed a significantly higher activity in altitude residents. It was concluded that the respiratory capacity of the muscle was apparently higher in natives living at high altitude than in those living at sea level. The enhanced enzymatic activity was probably related to the higher pigment content of the skeletal muscle. Results on myoglobin determinations in several other muscles from certain sea-level patients are discussed.