[A study on the physiological basis of training effect--with special reference to myoglobin. I. Isolation and properties of myoglobin from dog skeletal muscle (author's transl)].
Myoglobin (Mb) was isolated from canine skeletal muscle by a novel heat denaturation-gel filtration-ion exchange chromatography procedure. The purified major Mb was homogeneous by gel electrophoretic and ultracentrifugal analysis, and the sedimentation coefficient at infinite dilution (S degrees 20, w) was 1.9 S. The molecular weight by sedimentation equilibrium was 1.72 X 10(4) and was essentially identical with the values by the iron analysis (1.80 X 10(4) and the amino acid composition (1.78 X 10(4). The spectroscopic properties of deoxy-, oxy-, carbonmonoxy- and met-derivatives of the Mb were determined in ultraviolet, Soret and visible regions. The pK' of acid-alkaline transition of the met-Mb was estimated as 8.80+/-0.04 (25 degrees) from the pH-dependent spectral change. The oxygen equilibrium studies revealed complete absence of such allosteric properties as heme-heme interaction, anion effect and the Bohr effect which were always present in normal mammalian hemoglobins. Oxygen tension for the half-oxygenation was 0.48 mmHg (20 degrees) and its temperature-dependent change gave the delta H degrees of -15.7 Kcal/mole.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002498:Centrifugation; D004285:Dogs; D004592:Electrophoresis, Starch Gel; D006859:Hydrogen / Q000494:pharmacology; D066298:In Vitro Techniques; D007477:Ions; D007501:Iron / Q000032:analysis; D008970:Molecular Weight; D009211:Myoglobin / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D010101:Oxygen Consumption; D013054:Spectrophotometry, Atomic; D013696:Temperature
D000596:Amino Acids; D007477:Ions; D009211:Myoglobin; D006859:Hydrogen; D007501:Iron