Skinning effects on skeletal muscle myowater probed by T2 relaxation of 1H-NMR.
To find the cause of the skinning-induced fragility of frog skeletal muscle, the transverse relaxation process of 1H-NMR signals from skinned muscle was observed. A set of four characteristic exponentials well described the process. Aside from the extremely slow exponential component (time constant T2 > 0.4 s) representing surplus solution, the process was generally slower than that in living muscle. It had larger amplitudes of slow (T2 approximately 0.15 s) and intermediate (0.03 < T2 < 0.06 s) exponentials and had smaller amplitude and faster T2 in the rapid one (T2 < 0.03 s), suggesting that skinned muscle is more sol-like than intact myoplasm. To resolve their causes, we traced the exponentials following a stepwise treatment of living whole muscle to an isolated skinned fiber. Osmotic expansion of living muscle comparable to skinned muscle increased the intermediate exponential and decreased the rapid one without affecting T2. Subsequent chemical skinning markedly increased the slow exponential, decreased the rapid one, and slowed the intermediate one. The fiber isolation had no appreciable effect. Because l-carnosine at physiological concentration could not recover the skinning-induced difference, the difference would reflect the dilution and efflux of larger macromolecules, which stabilize myoplasm as a gel.
Takemori
Shigeru
S
Department of Physiology, The Jikei University School of Medicine, Tokyo 105-8461, Japan. sml@jikei.ac.jp
Yamaguchi
Maki
M
Kimura
Masako
M
D000818:Animals; D001834:Body Water / Q000737:chemistry* / Q000378:metabolism*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D018482:Muscle, Skeletal / Q000737:chemistry* / Q000378:metabolism*; D032383:Myocytes, Cardiac / Q000737:chemistry / Q000378:metabolism; D011522:Protons; D011898:Ranidae; D013048:Specimen Handling / Q000379:methods*; D014018:Tissue Distribution
D011522:Protons