• 제목/요약/키워드: Myofibril

검색결과 68건 처리시간 0.03초

동결 기간 및 해동 후 냉장이 제주 흑돼지고기의 물리화학적, 기호적 품질에 미치는 영향 (Effects of Freezing Period and Chilling Process after Thawing on Physicochemical Properties and Palatability of Loin from Jeju Island Reared Crossbred Black Pigs)

  • 문윤희
    • 동아시아식생활학회지
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    • 제20권4호
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    • pp.560-566
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    • 2010
  • 개량흑돼지(105~110 kg)를 도축한 후 약 18시간 냉장하고 등심육을 분할하여 진공 포장하고 $-20^{\circ}C$에서 1개월 및12개월 동결한 후 각각 $4^{\circ}C$에서 20시간 해동하였다. 해동 직후의 것(0-TP)과 해동 후 $2^{\circ}C$에서 2일간 냉장한 것(2-TP)의 물리화학적 및 기호적 특성을 비교하여 해동 후 냉장이 품질에 미치는 영향을 검토하였다. 개량흑돼지 등심육을 1개월간 동결하여 해동한 경우, 해동 직후의 0-TP보다 해동 후 냉장한 2-TP가 보수력 및 근원섬유 소편화 정도가 높아지고, 경도 및 씹힘성이 낮아졌으며, 가열육의 다즙성 및 종합적 기호도가 향상되었으나(p<0.05) 12개월 동결한 등심육은 해동 후 냉장에 의한 효과가 유의적으로 크지 않았다.

신경근전기자극이 스테로이드 투여 흰쥐의 골격근 무게 및 단백질 함량에 미치는 효과 (The Effect of Neuromuscular Electrical Stimulation(NMES) on Skeletal Muscle Weight and Myofibrillar Protein Content of Rats with Injection.)

  • 윤세원;신민철;정대인;김용남
    • 대한임상전기생리학회지
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    • 제1권1호
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    • pp.31-43
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    • 2003
  • The present studies are designed to determine whether the NMES can affect the muscle atrophy in rats following administration of steroid. Rats were divided into four groups: 1) Control group treated with administration of distilled water. 2) The group treated with administration of steroid. 3) The group treated with NMES once a day after adminstration of steroid. 4) The group treated with NMES twice a day after administration of steroid. The muscle atrophy was induced by one week administration of dexamethasone once a day by 3 mg/kg. The change in the structure of muscle fiber and the amount. of myofibril protein and gastrocnemius were determined after every week dissection of the tissues. The results were as follows; 1. The administration of steroid significantly affected the decrease in the weight, but NMES did not affect the inhibition of decrease in the weight. 2. The weight of gastrocnemius in the group once treated with NMES was changed two weeks later; similarly in the group twice treated with NMES significantly did two or three weeks later. These indicated that NMES affected the muscular activation of gastrocnemius(p<.05). 3. The changes in the amount of gastrocnemius protein by NMES might, indicate that NMES activated the capacity of synthesis of muscle fiber protein(p<.05).

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Analysis of Disease Progression-Associated Gene Expression Profile in Fibrillin-1 Mutant Mice: New Insight into Molecular Pathogenesis of Marfan Syndrome

  • Kim, Koung Li;Choi, Chanmi;Suh, Wonhee
    • Biomolecules & Therapeutics
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    • 제22권2호
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    • pp.143-148
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    • 2014
  • Marfan syndrome (MFS) is a dominantly inherited connective tissue disorder caused by mutations in the gene encoding fibrillin-1 (FBN1) and is characterized by aortic dilatation and dissection, which is the primary cause of death in untreated MFS patients. However, disease progression-associated changes in gene expression in the aortic lesions of MFS patients remained unknown. Using a mouse model of MFS, FBN1 hypomorphic mouse (mgR/mgR), we characterized the aortic gene expression profiles during the progression of the MFS. Homozygous mgR mice exhibited MFS-like phenotypic features, such as fragmentation of elastic fibers throughout the vessel wall and were graded into mgR1-4 based on the pathological severity in aortic walls. Comparative gene expression profiling of WT and four mgR mice using microarrays revealed that the changes in the transcriptome were a direct reflection of the severity of aortic pathological features. Gene ontology analysis showed that genes related to oxidation/reduction, myofibril assembly, cytoskeleton organization, and cell adhesion were differentially expressed in the mgR mice. Further analysis of differentially expressed genes identified several candidate genes whose known roles were suggestive of their involvement in the progressive destruction of aorta during MFS. This study is the first genome-wide analysis of the aortic gene expression profiles associated with the progression of MFS. Our findings provide valuable information regarding the molecular pathogenesis during MFS progression and contribute to the development of new biomarkers as well as improved therapeutic strategies.

Skeletal Ryanodine Receptor 1-Heterozygous PSE (Pale, Soft and Exudative) Meat Contains a Higher Concentration of Myoglobin than Genetically Normal PSE Meat in Pigs

  • Obi, T.;Matsumoto, M.;Miyazaki, K.;Kitsutaka, K.;Tamaki, M.;Takase, K.;Miyamoto, A.;Oka, T.;Kawamoto, Y.;Nakada, T.
    • Asian-Australasian Journal of Animal Sciences
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    • 제23권9호
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    • pp.1244-1249
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    • 2010
  • Comparisons of properties between skeletal ryanodine receptor 1 (sRyR1)-heterozygous-mutated and normal types of meat were carried out in pigs using PSE (pale, soft and exudative) meat found during the butchering process. All samples considered to be PSE meat showed irregular running and disorder of the muscle fibers and a wider inter-fiber space upon light microscopic observation. Electron microscopy revealed disintegration, twisting, and disorder of the myofibril arrangement and elimination of the Z line in PSE meat, compared with normal meat. Meat property tests demonstrated greater decreases in water holding capacity, moisture and sarcoplasmic protein, and higher $L^*$ values for the meat color index in PSE meat than in normal meat, but there were no differences in these factors between genetically normal and sRyR1-heterozygous PSE meat. On the other hand, higher $a^*$ and $b^*$ values were observed in sRyR1-heterozygous than in normal PSE meat, and similar alterations to the a* value were observed in terms of the amount of myoglobin and density of the 17-kDa protein band, corresponding to the molecular mass of myoglobin, on SDS-PAGE gels. These results suggest that sRyR1-heterozygous PSE pork contains much more myoglobin than genetically normal PSE meat.

Nebulin C-terminus Interacts with NCBP51, a New Isoform of RING Finger Protein 125 (RNF125)

  • Kim, Ji-Hee;Kim, Hyun-Suk;Park, Eun-Ran;Choi, Jae-Kyoung;Lee, Yeong-Mi;Choi, Jun-Hyuk;Shin, Jung-Woog;Kim, Chong-Rak
    • 대한의생명과학회지
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    • 제13권1호
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    • pp.1-10
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    • 2007
  • Nebulin, a giant modular protein from muscle, is thought to act as molecular ruler in sarcomere assembly. In skeletal muscle, the C-terminal ${\sim}50 kDa$ region of nebulin extends into the Z-line lattice. The most recent studies implicated highlighting its extensive isoform diversity and exciting reports revealed its expression in cardiac and non-muscle tissues containing brain. Also these novel findings are indicating that nebulin is actually a multifunctional filament system, perhaps playing roles in signal transduction, contractile regulation, and myofibril force generation, as well as other not yet defined functions. However the binding protein of nebulin and function in brain is still unknown. A novel binding partner of nebulin C-terminal region was identified by screening a human brain cDNA library using yeast two-hybrid system. Nebulin C-terminus binding protein 51 (NCBP51) was contained a RING-finger domain and identified a new isoform of RING finger protein 125 (RNF125). The interaction was confirmed using the GST pull-down assay. NCBP51 belongs to a family of the RING finger proteins and its function remains to be identified in brain. The role of nebulin and NCBP51 will be studied by loss-of-function using siRNA technique in brain.

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Marination and Physicochemical Characteristics of Vacuum-aged Duck Breast Meat

  • Khan, Muhammad Issa;Lee, Hyun Jung;Kim, Hyun-Joo;Young, Hae In;Lee, Haelim;Jo, Cheorun
    • Asian-Australasian Journal of Animal Sciences
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    • 제29권11호
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    • pp.1639-1645
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    • 2016
  • We investigated marinade absorption and physicochemical characteristics of vacuum-aged duck breasts that were halved and individually vacuum-packed for chiller aging at $4^{\circ}C$ for 14 d. One half was marinated for 0, 7, or 14 d, while the second half was used as a control. Marinade absorption, cooking loss, cooking yield, texture profile, pH, color, protein solubility, and thiobarbituric acid reactive substances (TBARS) values were evaluated, and protein sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed. Marinade absorption and pH did not vary significantly after 14 d of aging. Marination increased the pH, color ($a^*$ and $b^*$) values, and cooking yield and reduced cooking loss. TBARS values significantly increased with aging time, but were significantly reduced by marination. Myofibril and total protein solubility increased with aging and marination, while SDS-PAGE showed protein degradation. Hence, aging and marination can be used simultaneously to improve physicochemical quality and cooking yield of vacuum-aged duck breast.

고온숙성에 의한 저급육의 연도개선과 그 이용 (Tenderness Improvement and Utilization of Low Quality Meat by High Temperature Aging)

  • 성삼경
    • 한국식품과학회지
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    • 제21권4호
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    • pp.549-555
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    • 1989
  • 저급육인 한우숫소의 앞다리고기를 도살직후 $16{\pm}2^{\circ}C$에서 고온숙성하여 연도개선 효과를 검토하였다. 또한 24시간 고온숙성한 후, 재구성육을 조제하여 결착성 개선방법을 모색하였다. 시료의 처리는 소금(0, 0.5, 1.0%), pyrophosphate(0, 0.3, 0.5%)와 이들의 혼용효과를 검토하였고, 소금(0.5%)과 pyrophosphate(0.3%)를 혼용한 원료에 succinic anhydride(0, 0.1, 0.2, 0.3%)를 첨가하여 석시닐산의 첨가효과를 검토하였다. 얻어진 결과는 다음과 같다. 1. 고온숙성은 저온숙성에 비하여 전단력이 낮았고, 근원섬유소편화지수가 높았으며, 연도개선의 효과가 뛰어났다. 전자현미경에 의한 형태학적 변화의 결과도 이들 결과 일치하였다. 2. 재구성육의 파단응력은 소금과 인산염의 첨가수준이 증가할수록 높아졌고, 소금과 인산염을 혼용할 경우, 현저히 증가하였다. 3. 조리수율은 소금과 인산염의 첨가수준이 증가할수록 낮아졌고, 소금과 인산염을 혼용할 경우, 현저하게 감소하였다. 4. TBA가는 소금 첨가수준에 비례하여 증가하였으며, 인산염 및 인산염과 소금혼용의 경우는 약간 증가하는 경향이었다. 5. 석신산은 재구성육의 결착력과 품질개선에 전혀 도움이 되지 않았다.

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Meat quality characteristics of the Arabian camel (Camelus dromedarius) at different ages and post-mortem ageing periods

  • Suliman, Gamaleldin Mustafa;Al-Owaimer, Abdullah Naser;Hussein, Elsayed Osman Swelum;Abuelfatah, Kamaleldin;Othman, Moath Badr
    • Asian-Australasian Journal of Animal Sciences
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    • 제33권8호
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    • pp.1332-1338
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    • 2020
  • Objective: Meat quality characteristics and sensory attributes were evaluated in three age groups (12, 18, and 24 mo) of one-humped camels of the Saudi Arabian Najdi breed. Methods: Thirty-six male camels (12 for each age group) were used. The Longissimus dorsi muscle from each carcass was divided into three parts and subjected to three ageing periods (1, 5, or 10 d) and evaluated for shear force, myofibril fragmentation index (MFI), expressed juice, cooking loss, and sensory attributes. Results: Age had a significant effect on shear force, MFI, expressed juice quantity, and organoleptic properties. Camels slaughtered at 12 mo exhibited lower shear force and MFI, and higher expressed juice quantity, tenderness, juiciness, and overall acceptability than those slaughtered at 24 mo. Ageing had a significant influence on shear force, MFI, expressed juice quantity, but not on cooking loss. Camel meat aged for 10 d exhibited significantly lower shear force values and expressed juice quantity, and significantly higher MFI compared to that aged for 1 d. However, ageing did not significantly affect sensory attributes, except for tenderness, in camels slaughtered at 18 mo. Conclusion: Both instrumental and sensory evaluations showed that young camel meat has desirable quality characteristics, with superior tenderness and juiciness.

사후강직형태에 따른 근원섬유 단백질의 이화학적 성질변화 (Postmorten Changes in the Myofibrillar Proteins of Alkaline and Acid Rigor Rabbit Muscle during Storage)

  • 김대곤;성삼경
    • 한국식품영양과학회지
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    • 제21권6호
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    • pp.712-718
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    • 1992
  • 산 강직근과 알카리 강직근의 사후 자장중 물리, 화학적 변화를 비교 검토하였다. 근섬유의 소편화도는 산강직근이 알카리 강직근에 비하여 저장 3일째부터 월등히 높았다. $Mg^{2+}$-ATPase 활성은 알카리 강직근이 저장 전기간 동안 산 강직근 보다 높았으며, 산 강직근은 저장 1일째, 알카리 강직근은 저장 3일째에 가장 높았다. $Ca^{2+}$-ATPase 활성에 있어서 산 강직근과 알카리 강직근 모두 전 저장기간 동안 약간 증가하는 경향이었으나 산 강직근은 알카리 강직근 보다 전기간 동안 활성도가 낮았다. Actomyosin의 용해성이나 myofibril의 전기영동상은 강직 형태에 따른 유의한 차이가 없었다.

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오리고기의 근원섬유 단백질에 관한 연구 (Studies on the Myofibrilar Protein from Korean Duck Muscle)

  • 장인애;남현근
    • 한국식품영양과학회지
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    • 제9권1호
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    • pp.45-50
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    • 1980
  • 우리나라에서 사육되는 오리고기로 부터 Myofibrillar protein 을 추출하여 생채 촉매인 ATPase의 활성을 조사한 결과는 다음과 같다. 1. Mg- activated ATPase 활성은 이온 강도가 낮을때 활성은 증가하고 이온농도가 높으면 활성은 감소되었으며 바다오리와 사육장오리고기 사이에 차이가 있었다. 2. Myofibrillar protein 의 ATPase 활성에 EDTA의 영향은 $4.6{\mu}g$ 을 넣었을때 ATPase 활성은 오히려 증가 되었으나 $6.9{\mu}g$ 이상인때 활성이 감소되었다. 3. Myofibrillar protein의 ATPase 활성에 $Ca^{++}$ 의 영향은 $3{\mu}g$ 이상을 첨가할때 활성이 현저히 감소되었다. 4. Myofibrillar protein의 ATPase 활성에 $Mg^{++}$의 영향은$3.6{\mu}g$ 을 첨가하면서 활성은 현저히 감소되었다. 사사: 본 실험을 수행하는데 수고한 조교 임경애의 노고에 감사한다.

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