• Korean Journal of Food Science and Technology
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• v.6 no.4
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• pp.199-208
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• 1974

An attempt was made to study on new method for the extraction of the regulatory proteins from myofibrils, and the procedures for the preparation of desensitized actomyosin and for complete extraction of troponin-tropomyosin complex were developed. When myofibrils were treated through the procedures developed in this study, actomyosin obtained had no Ca-sensitivity, indicating that Ca-sensitizing protein factor had been removed completely from myofibril. Consequently, it was concluded that the procedures developed in this study were convenient to test whether Ca-sensitizing proteins has been removed or not. When Mg-activated ATPase activity of myofibril were measured, the myofibrillar ATPase turned into the actomyosin type ATPase with the progress of the treatment. This result was interpreted to show that the regulatory proteins of the myofibril seems to play a cementing role on the structure of myofibril. When supernatant containing the regulatory proteins were fractionated with $(NH_4)_2SO_4$ saturation solution, regulatory proteins, ${\alpha}-actinin$ and troponia-tropomyosin complex, could be obtained and they showed their typical phyoislogical activity which modify the actin-myosin interaction. The amount of troponin-tropomyosin complex in myofibril was 72 mg per g myofibril. This result was in good agreement with the results reported by many investigators, and therefore it was concluded that our procedures for the extraction of troponin-tropomyosin complex were desirable to study on the quantitative analysis of troponin-tropomyosin complex.

• Journal of Life Science
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• v.22 no.3
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• pp.398-406
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• 2012

This study aimed to examine whether the polygenic profile of ACE ID and ACTN3 R577X polymorphisms is associated with muscle power performance in Korean athletes. For this study, 106 top-class power athletes (top-class group), 158 elite power athletes (elite-class group), and 676 healthy adults (control) aged 18-39 yrs were recruited and their genotypes were analyzed. The top-class group showed higher frequencies of the II genotype and I allele in ACE, as well as higher frequencies of the RR genotype and R allele in ACTN3 (top-class vs. control: 41.4% vs. 32.1% for II genotype, 67.1% vs. 57.7% for I allele, p<0.05; 42.3% vs. 29.0% for RR genotype, 65.3% vs. 54.8% for I allele, p<0.05). In the polygenic profile, the top-class group had significantly higher frequencies of combined-II/ID+RR/RX genotype than the control group (top-class vs. control: 82.9% vs. 66.7% for II/ID+RR/RX, p<0.05), and there was even a sharp increase in total genotype score (TGS) in this group compared to the elite-class and control groups ($66{\pm}0.9$ vs. $58{\pm}1.9$ vs. $56{\pm}2.3$, p<0.05). The combined-II/ID+RR/RX genotype showed the possibility of succussion in the top-class muscle power performance with an odds ratio of 2.3 (CI:1.4-4.1, p<0.05). These results suggested that ACE and ACTN3 need to interact with each other to affect muscle-power performance in an additive form. Furthermore, the polygenic profile of ACE and ACTN3 can predict muscle performance with high success in a homogeneous dominant combined genotype (II/ID+RR/RX). A further study could identify and combine other genes into ACE and ACTN3 for muscle strength.