caa a22 4500 467953082 CHVBK 20180323165703.0 cr unu---uuuuu 170328e19891001xx s 000 0 eng 10.1007/BF02396155 doi (NATIONALLICENCE)springer-10.1007/BF02396155 (NATIONALLICENCE)springer-10.1007/BF00553635 Variation among lines selected for body size in the fractional rate of degradation of protein and acid protease activity in the muscle of quail ( Coturnix coturnix japonica ) [Elektronische Daten] [Yoshizane Maeda, Makoto Fujii, Shin Okamoto, Tsutomu Hashiguchi] Fractional rates (%/day) of degradation of muscle protein were determined by measuring the output of Nτ-methylhistidine (Nτ-MH) in the excreta at 2 and 10 weeks of age in three lines of quail, a random-bred line and two lines selected for body size, one for increased and the other for decreased size. In all lines, fractional rates of degradation of muscle protein at 2 weeks of age were higher than those at 10 weeks of age. The fractional rate of degradation at 2 weeks of age was highest for the RR line, 9.1-9.2%/day. However, at 10 weeks of age, the rank order changed, and the RR line showed the lowest rate, 1.8-1.9%/day. The SS line (5.8-6.2%/day at 2 weeks and 5.8-5.9%/day at 10 weeks of age) was significantly higher than the LL line (4.1-4.2%/day at 2 weeks and 2.1-2.2%/day at 10 weeks of age). Acid protease activities in supernatants of homogenized muscle of the three lines of quail at 2 and 10 weeks of age were measured. In all lines, the acid protease activities in supernatant of homogenized muscle decreased from 2 to 10 weeks of age. At 2 weeks, the protease activity of the RR line was significantly higher than that of the LL and SS lines, which did not differ significantly. However, at 10 weeks of age, the SS line had higher activity in both sexes than the LL and RR lines. The results suggest that selection for body size brings about significant changes in both fractional degradation rate and acid protease activity in the muscle. Plenum Publishing Corporation, 1989 muscle protein nationallicence protein turnover nationallicence degradation nationallicence protease nationallicence Maeda Yoshizane Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut Fujii Makoto Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut Okamoto Shin Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut Hashiguchi Tsutomu Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut Biochemical Genetics Kluwer Academic Publishers-Plenum Publishers 27/9-10(1989-10-01), 603-611 0006-2928 27:9-10<603 1989 27 10528 https://doi.org/10.1007/BF02396155 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02396155 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Maeda Yoshizane Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut NATIONALLICENCE 700 1- Fujii Makoto Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut NATIONALLICENCE 700 1- Okamoto Shin Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut NATIONALLICENCE 700 1- Hashiguchi Tsutomu Department of Animal Science, Faculty of Agriculture, Kagoshima University, 890, Kagoshima, Japan aut NATIONALLICENCE 773 0- Biochemical Genetics Kluwer Academic Publishers-Plenum Publishers 27/9-10(1989-10-01), 603-611 0006-2928 27:9-10<603 1989 27 10528 NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00553635 text/html Onlinezugriff via DOI Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE NATIONALLICENCE NL-springer