• 한국식품영양과학회지
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• 제23권5호
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• pp.827-831
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• 1994

Investigation on the extractability, Mg2+-, Ca2+ , EDTA-ATPase activity and solubility of actomyosin prepared from leg and breast muscle of silky fowol were as follows. The extractability of actomyosin in leg and breast muscle was 779mg/100g and 1, 318mg/100g respectively, breast muscle was higher than leg muscle . Mg2+-ATPase activity of actomyosin was high inionic strength 0.02-0.10 and Mg2+ATPase activity of low ionic strength was higher than high ionic strength not related to the part. Ca2+ ATPase activity was high in ionic strength 0.05-0.13, the activity of leg muscle was higher that breast muscle. And EDTA-ATPase activity showed low in low ionic strength and showed high in high ionic strength, and increased greatly depend ionic strength up to 0.4. The solubility of actomyosin was not different in leg and breast muscle , the solution started in KCI concentration of 0.3M and ended in DCI concentration of 0.4M.

• 한국축산식품학회지
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• 제23권3호
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• pp.193-199
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• 2003

본 연구는 배, 파인애플, 키위로부터 획득한 단일 단백질 분해효소 또는 이들의 혼합 단백질분해효소의 pH 및 처리시간에 따른 계육의 actomyosin분해 능력에 미치는 영향을 조사하였다. 파인애플 단백질분해효소를 처리한 경우, pH 5.3, 7.0과 8.0 모두에서 가장 강한 분해능력을 나타내었으나, 배 및 키위 단백질분해효소의 actomyosin 분해 능력은 비슷한 경향을 보였다. pH에 따른 분해 능력의 조사 결과는 배, 파인애플 및 키위 단백질분해효소 모두pH 5.3에서 강한 분해 활성을 나타내었으나, pH 8.0에서는 파인애플을 제외한 배 및 키위 단백질분해효소는 약한 분해 반응을 보였다. 배 단백질분해효소와 파인애플 단백질분해효소를 1:1 (w/w)로 혼합하였을 때 pH조건에 크게 영향을 받지 않고 강한 분해를 나타낸 반면, 배와 키위 단백질분해효소의 혼합 또는 키위 와 파인애플 단백질분해효소의 혼합의 경우, 배와 파인애플 단백질분해효소의 혼합의 경우에 비해 분해 능력이 낮아지는 것으로 나타나, pH 7.0에서는 키위 효소의 단백질 분해 활성은 배 단백질분해효소와는 영향을 받지 않으나 파인애플로부터 추출한 단백질분해효소와는 경합적으로 작용하는 것으로 관찰되었다. 한편, 배, 파인애플 및 키위 단백질 분해효소의 혼합효소로 처리한 경우pH의 차이에 크게 영향을 받지 않으며 이상적인 분해 능력을 나타내었다. 따라서, 본 연구 결과, 파인애플 및 파파야 등 열대 과일 유래의 단백질분해효소 단일로 처리할 때의 단점인 과잉분해의 문제점이 배 단백질분해효소의 혼합이용을 통해 개선될 수 있는 가능성을 제시하였다.

• 한국식품영양과학회지
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• 제21권4호
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• pp.348-352
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• 1992

오리를 고온침탕법과 중온침탕법에 의해 털을 제거하고 다리 및 가슴부위의 골격근에서 actomyosin을 추출하여 몇가지 특성을 비교하엿다. 고온침탕 처리한 근육으로부터 추출된 actomyosin의 추출성은 다리와 가슴근육이 각각 7.84, 39.48mg/g, 중온침탕한 것은 각각 4.79, 28.04mg/g고온침탕법의 추출성이 더 높았다. Actomyosin의 $Ca^{2+}-ATPase$ 활성은 고온침탕법이 다리근육의 경우에서는 중온침탕법보다 낮았으나 가슴근육은 이온강도 0.08 이하에서 중온침탕법이 높았고 그 이상에서는 고온침탕법이 높았다. Actomyosin의 $Mg^{2+}-ATPase$ 활성은 저이온강도에서 활성이 컸으며 가슴근육이 다리근육의 경우보다 침탕법에 의한 활성의 차이가 크게 나타났다. 용해도는 침탕방법과 부위에 관계없이 용해시점과 완료시점이 비슷하였다. 그리고 고온침탕 처리한 근육과 다리보다 가슴근육이 thin filament에 있는 단백질이 많이 추출되어 나오는 현상을 보였다.

• Journal of Nutrition and Health
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• 제11권3호
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• pp.37-42
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• 1978

Actomyosin and myofibril were extracted from Korean native Goat muscle with the Weber-Edsall solution. ATPase activities and physiochemical properties were measured. The results obtained were as follows; 1) Mg-activitied ATPase activity of actomyosin and myofibrill from Korean native Goat muscle exhibited a common biphasic response, a typical ATPase pattern, that is high at a low ionic strength and low at a high ionic strength. Actomyosin showed high activity than myofibrill. 2) Mg-activited ATPase activity of actomyosin from muscle increased extraction time 24 hours. 3) EDTA-enhanced ATPase activity of actomyosin was greater than myofibrill and low at the low ionic strength, high at the high ionic strength. The difference of the activity were shown great broad pattern at the after 0.3M KCI concentration. 4) Effect of EGTA on-ATPase activity of myofibrill and actomyosin from muscle was measured, the Mg-ATPase activity was markedly depressed. 5) Solubility of actomyosin from muscle began to solubilize at KCI concentration of 0.28M and solubilized completely at the KCI concentration of 0.3M.

• 한국식품영양과학회지
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• 제19권4호
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• pp.349-355
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• 1990

Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.

• The Korean Journal of Physiology
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• 제11권2호
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• pp.1-7
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• 1977

The activity of the $Ca^{++}$ activated adenosinetriphosphatase (Ca-ATPase) of actomyosin systeme of rabbit and frog skeletal muscle has been studied at varying pH and temperature. The PH optima of the Ca-ATPase activity of the rabbit actomyosin was rather broad. Over the temperature range of $16-36^{\circ}C$ activity of the enzyme was not appreciably changed between pH 6.4-8.5; below and above which it rapidly reduced. The pH at the inflection point of the enzyme activity increased as temperature decreased, showing the ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ of approximately $-0.018\;unit/^{\circ}C$. Consequently, $(OH^-)/(H^+)$ ratio at the inflection point was constant regardless of assay temperature. In the frog actomyosin systems the Ca-ATPase activity was not apparently altered between PH 6.4-7.0 when the incubation temperature was $15{\sim}30^{\circ}C$. Outside of this range of pH, however, the enzyme activity was dramatically decreased. The pH of the inflection point changed inversely with temperature. ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ at the acidic side was approximately $-0.018\;unit/^{\circ}C$, whereas that at the alkaline side it was about $-0.037\;unit/^{\circ}C$. The Arrhenius Plot on the Ca-ATPase activity at constant $(OH^-)/(H^+)$ ratio of 1.0 was not linear, but showed break at arround $20^{\circ}C$ for both rabbit and frog actomyosin Preparations. From these results it was speculated that pH dependence of Ca-ATPase activity of rabbit actomyosin systems might reflect titrations of histidine-imidazole and -SH groups, and that of the frog actomyosin represents titrations of histidine-imidazole and lysyllysine ${\alpha}-NH_2$ groups.

• 한국수산과학회지
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• 제5권2호
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• pp.57-62
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• 1972

잉어의 배육 골격근에서 actomyosin을 추출하여 몇 가지 생물물리화학적인 성질을 측정 검토한 결과는 다음과 같다. 즉, actamyosin의 침강 정수($s_{20},\;_\omega$)는 24.76s이고 그 점성은 단백 농도의 증가와 더불어 급상승하여 다른 actomyosin의 그것과 비숫한 경향을 보였다. 그리고, ATP-sensitivity는 $147\~176$이었고, PH영향하에서 ATPase activity는 산성측이 6,0부근, 알칼리성측이 9.5부근이었으므로 ATPase activating site가 산, 알칼리 양측에 있음을 알았다.

• 한국식품영양학회지
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• 제10권2호
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• pp.160-165
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• 1997

오징어의 actomyosin과 myosin은 3$0^{\circ}C$에서 최대 Vmax를 나타냈고 대합의 actomyosin과 myosin은 35$^{\circ}C$에서, HMM은 $25^{\circ}C$에서 최대 Vmax를 보였다. 또한 근원섬유단백질의 열 안정성은 염농도의 차이에 따라 크게 변하여 염농도가 높을수록 변성의 정도가 컸으며 대합의 근원섬유단백질이 오징어의 근원섬유단백질보다 높은 열 안정성을 나타냈다. 근원섬유단백질에 3%의 에탄올을 첨가하여 가온하면 변성은 가속화되었으며 변성속도에 있어서도 동물간에 차이가 있는 것으로 나타났다.

• 동아시아식생활학회지
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• 제16권4호
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• pp.453-457
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• 2006

This study investigated the extractability, solubility, Mg$^{2+}$-, Ca$^{2+}$- and EDTA-ATPase activity of actomyosin prepared from leg and breast muscle of dog meat. The actomyosin extractability of breast muscle(2,100.6 mg/l00 g) was higher than that of leg muscle(500.8 mg/l00 g). The Mg$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.05 M KCI and did not differ between leg and breast muscle. The Ca$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.10 M KCI and leg muscle had a higher level of Ca$^{2+}$-ATPase activity than breast muscle did. The EDTA-ATPase activity was lower in low ionic strength and showed higher in high ionic strength, and increased sharply with increasing ionic strength up to 0.3 M KCI. The solubility of actomyosin did not differ between leg and breast muscle, and the solubility started and ended at KCI concentrations of 0.35 M and 0.4 M, respectively.

• 한국식품영양과학회지
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• 제14권1호
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• pp.77-81
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• 1985

사양기간(飼養期間)이 서로 다른 닭의 골격근에서 actomyosin 을 추출하여 추출성과 생물 활성을 비교하였다. 가슴부위에서 추출한 actomyosin의 추출성은 사양기간(飼養期間)이 3,4,5,6,7주(週)의 순으로 각각 184.5, 364.0, 784.8, 926.1, 985.2, 1020.1 mg/100g 이었고 다리부위는 각각 28.6, 70.8, 137.9, 139.5, 608.3 그리고 646.2mg/100g 이었다. 사양기간(飼養期間)이 3,6,8주(週)인 경우 24시간 추출한 actomyosin의 EDTA-ATPpase활성은 각각 0.68, 0.59, 0.50${\mu}M$ Pi/mg protein min. 이었고 Mg^{+2}$-ATPase 활성은 각각 0.66, 0.71, 0.75 $0.50\;{\mu}M$ Pi/mg protein min.이었고 Mg^{+2}$-ATPase 활성은 각각 0.66, 0.71, $0.75\;{\mu}moles$ Pi-mg protein/min.이었다. 사양기간(飼養期間)에 관계없이 actomyosin 의 3, 6, 8 Mg^{+2}$-ATPase 활성은 저(低) ion 강도에서 높은 활성과 rh(高) ion 강도에서 낮은 biphasic response를 나타내었고 $125\;{\mu}mole$ EGTA로서 Mg^{+2}$-ATPase 활성을 $0.1\;{\mu}mole/mg$ protein/min 이하로 저해시켰다.