• 제목/요약/키워드: sarcoplasmic proteins

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동면 전ㆍ후 짱뚱어의 육단백질 및 아미노산 조성의 변화에 관한 연구 (The Study in the Composition Changes of Muscle Proteins and Amino Acids in the Hibernant Fish-Mudskipper (Boleophthalmus pectinirostris) before and after Hibernation)

  • 박일웅
    • 한국식품영양학회지
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    • 제16권3호
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    • pp.209-217
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    • 2003
  • 동면어 짱뚱어에 대해 월동전ㆍ후(성숙기: 8월, 동면직전: 11월, 동면직후: 4월) 육단백질과 유리아미노산 조성 등을 각 시기별로 비교, 검토하였다. 조단백질 함량은8월 17.8%, 11월 17.5%, 4월 16.9%이었고 근원질 단백질은 육단백질 전체의 19.2~20.4%, 근원섬유 단백질은 58.8~61.3%, 세포내 잔사단백질과 기질단백질은 각각 11.2~13.2%와 7.5~8.3%를 차지하였다. 단백질 조성을 시기별로 비교한 결과 11월까지는 거의 차이가 없으나 4월은 기질단백질을 제외한 근원질과 근원섬유단백질 2종이 소량 줄었고 조성비로 근원질단백의 감소가 조금 더 큰 것으로 파악되었다. 근원질단백 구성 subunit는 총 14종이 검출되었고 구성 subunit 중 30kDa와 46kDa등의 조성이 11월보다 4월에 소폭 증가하였고 35kDa, 65kDa 등은 소폭 감소하였으나 기타 대부분은 거의 차이가 없었다. 근원섬유단백질은 총 13개의 subunit가 검출되었고 대부분의 subunit 조성이 11월까지는 거의 비슷하였으나 4월은 동면전보다 myosin heavy chain 조성이 3% 정도 늘어난 반면 actin은 3%정도 줄어들었다. 단백질 구성 아미노산 조성은 전기간에 걸쳐 일정하였고 주요 유리아미노산은 glycine과 alanine이었으며 두드러진 특징은 arginine함량이 8월보다 11월이 2배, 4월은 4배 이상 늘었고 glycine도 8월보다 4월이 2배 함량으로 모든 아미노산 중 양적 증가가 가장 현저하였다. 기타 alanine, glutamic acid, serine 및 aspartic acid와 valine 등도 동면기간 상당폭으로 증가하였고 lysine, histidine 등의 필수아미노산 함량도 유의적으로 증가하였다.

The Effect of Irradiation on Meat Products

  • Yea-Ji Kim;Ji Yoon Cha;Tae-Kyung Kim;Jae Hoon Lee;Samooel Jung;Yun-Sang Choi
    • 한국축산식품학회지
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    • 제44권4호
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    • pp.779-789
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    • 2024
  • The effects of irradiation on meat constituents including water, proteins, and lipids are multifaceted. Irradiation leads to the decomposition of water molecules, resulting in the formation of free radicals that can have both positive and negative effects on meat quality and storage. Although irradiation reduces the number of microorganisms and extends the shelf life of meat by damaging microbial DNA and cell membranes, it can also accelerate the oxidation of lipids and proteins, particularly sulfur-containing amino acids and unsaturated fatty acids. With regard to proteins, irradiation affects both myofibrillar and sarcoplasmic proteins. Myofibrillar proteins, such as actin and myosin, can undergo depolymerization and fragmentation, thereby altering protein solubility and structure. Sarcoplasmic proteins, including myoglobin, undergo structural changes that can alter meat color. Collagen, which is crucial for meat toughness, can undergo an increase in solubility owing to irradiation-induced degradation. The lipid content and composition are also influenced by irradiation, with unsaturated fatty acids being particularly vulnerable to oxidation. This process can lead to changes in the lipid quality and the production of off-odors. However, the effects of irradiation on lipid oxidation may vary depending on factors such as irradiation dose and packaging method. In summary, while irradiation can have beneficial effects, such as microbial reduction and shelf-life extension, it can also lead to changes in meat properties that need to be carefully managed to maintain quality and consumer acceptability.

Physico-chemial Properties of Pacific Whiting Surimi by Acid-Aided Processing

  • Park, Y.J.;Kim, B.J.;Lee, K.W.;Y.J. Cho;Park, J.W.
    • 한국어업기술학회:학술대회논문집
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    • 한국어업기술학회 2000년도 추계수산관련학회 공동학술대회발표요지집
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    • pp.79-80
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    • 2000
  • Conventional surimi processing from white flesh fish, such as Pacific whiting and Alaska Pollee utilizes only <25% of the body (Toyoda and others 1992; Park and others 1997). Conventional surimi is refined myofibrillar proteins processed by removing unnecessary foreign materials such as fat, pigment skin, and water soluble sarcoplasmic proteins. The acid-aided process demonstrated excellent gel forming ability for cod and mackerel with extremely higher yield (Hultin and Kelleher 1999). (omitted)

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Changes in the Expressional Levels of SR $Ca^{2+}$ Regulatory Proteins of Hypertensive Rats

  • Park, Miyoung;Lee, Eun-Hee;Lee, Hee-Ran;Kim, Hae-Won
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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    • pp.53-53
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    • 1999
  • We have investigated whether alterations in the expression levels of sarcoplasmic reticulum (SR) $Ca^{2+}$ regulatory proteins in heart and mesenteric arteries from different models of hypertension would occur. Nephrectomied diabetic-hypertensive rats (DM-HT) and spontaneously hypertensive rats (SHR) were used as models of hypertension.(omitted)

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Evaluation of Acid-treated Fish Sarcoplasmic Proteins on Physicochemical and Rheological Characteristics of Pork Myofibrillar Protein Gel Mediated by Microbial Transglutaminase

  • Hemung, Bung-Orn;Chin, Koo Bok
    • 한국축산식품학회지
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    • 제35권1호
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    • pp.50-57
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    • 2015
  • Fish sarcoplasmic protein (SP) is currently dumped as waste from surimi industry and its recovery by practical method for being the non-meat ingredient in meat industry would be a strategy to utilize effectively the fish resource. This study was aimed to apply pH treatment for fish SP recovery and evaluated its effect on pork myofibrillar protein (MP) gel. The pH values of fish SP were changed to 3 and 12, and neutralized to pH 7 before lyophilizing the precipitated protein after centrifugation. Acid-treated fish SP (AFSP) showed about 4-fold higher recovery yield than that of alkaline-treated SP and water absorption capacity was also about 1.2-fold greater. Because of the high recovery yield and water absorption capacity, AFSP was selected to incorporate into MP with/without microbial transglutaminase (MTG). The effects of AFSP and MTG on the physicochemical and rheological characteristics of MP and MP gel were evaluated. MTG induced an increase shear stress of the MP mixture and increase the breaking force of MP gels. MP gel lightness was decreased by adding AFSP. MP gel with MTG showed higher cooking loss than that without MTG. A reduction of cooking loss was observed when the AFSP was added along with MTG, where the insoluble particles were found. Therefore, AFSP could be contributed as a water holding agent in meat protein gel.

Quality properties of whole milk powder on chicken breast emulsion-type sausage

  • Kang, Kyu-Min;Lee, Sol-Hee;Kim, Hack-Youn
    • Journal of Animal Science and Technology
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    • 제63권2호
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    • pp.405-416
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    • 2021
  • The aim of the study was to determine the effect of whole milk powder (WMP) as heterologous proteins on chicken breast emulsion-type sausages. The quality properties of WMP on such chicken breast emulsion-type sausages were investigated by measuring the proximate composition, pH, color, cooking yield, protein solubility, and by applying other methods, such as texture profile analysis (TPA), microphotograph, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and electronic nose. The crude fat, protein, and ash contents of 15% WMP samples were significantly higher than the control samples (p < 0.05). The redness of the cooked samples significantly increased with an increase in the WMP contents (p < 0.05). The cooking yield of WMP treated samples was significantly higher than the control sample (p < 0.05). Additionally, the hardness, gumminess, and chewiness of WMP treated samples were significantly higher than the control sample (p < 0.05). The sarcoplasmic and myofibrillar proteins of samples containing 15% WMP were significantly higher than the control samples (p < 0.05). The result of SDS-PAGE showed that the C protein, sarcoplasmic protein, actin, and tropomyosin increased with an increase in the WMP contents. The principal component analysis plot of WMP-treated samples was clearly different from that of the control samples. Based on these results, it was predicted that WMP could be useful as heterologous protein on emulsion-type sausage.

Molecular Properties of Excitation-Contraction Coupling Proteins in Infant and Adult Human Heart Tissues

  • Jung, Dai Hyun;Lee, Cheol Joo;Suh, Chang Kook;You, Hye Jin;Kim, Do Han
    • Molecules and Cells
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    • 제20권1호
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    • pp.51-56
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    • 2005
  • Excitation-contraction coupling (ECC) proteins in the human heart were characterized using human atrial tissues from different age groups. The samples were classified into one infant group (Group A: 0.2-7 years old) and three adult groups (Group B: 21-30; Group C: 41-49; Group D: 60-66). Whole homogenates (WH) of atrial tissues were assayed for ligand binding, $^{45}Ca^{2+}$ uptake and content of ECC proteins by Western blotting. Equilibrium [$^3H$]ryanodine binding to characterize the ryanodine receptor (RyR) of the sarcoplasmic reticulum (SR) showed that the maximal [$^3H$]ryanodine binding ($B_{max}$) to RyR was similar in all the age groups, but the dissociation constant ($k_d$) of ryanodine was higher in the infant group than the adult groups. Oxalate-supported $^{45}Ca^{2+}$ uptake into the SR, a function of the SR SERCA2a activity, was lower in the infant group than in the adult groups. Similarly, [$^3H$]PN200-110 binding, an index of dihydropyridine receptor (DHPR) density, was lower in the infant group. Expression of calsequestrin and triadin assessed by Western blotting was similar in the infant and adult groups, but junctin expression was considerably higher in the adult groups. These differences in key ECC proteins could underlie the different $Ca^{2+}$ handling properties and contractility of infant hearts.

방어 보통육과 혈합육의 단백질 및 아미노산조성의 사후변화 (Changes Occurred in Protein and Amino Acid Compositions during Postmortem Aging of White and Dark Muscle of Yellowtail at $2^{\circ}C$)

  • 김장양;최영준;변재형
    • 한국수산과학회지
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    • 제15권2호
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    • pp.123-136
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    • 1982
  • 방어의 배육 보통육과 측육 혈합육을 $2^{\circ}C$에 보장하여 두고 선도변화 총계별로 단백질의 조성과 각축의 구성 및 유리아미노산의 조성을 분석하였으며, 건향질단백질과 근원섬유단백질에 대하여는 구성단백질의 분포변화를 확인하기 위하여 $NaDodSO_4$변한 다음, polyacrylamide겔 전기영동상을 비교 해석함으로써 적색육어류의 선도변화와 보통육 및 혈합육의 단백질조성 변화와의 관련성을 검토하였다. K-값과 휘발성염기질소 및 pH값으로 판정했을 때, 혈합육은 보통육에 비하여 선도변화가 빨랐다. 사후 선도변화와 더불어 근원질단백질과 노원섬유단백질은 감소하는 반면, 세포내잔사단백질은 상대적으로 증가하였으며, 이러한 변화는 보통육에 비하여 혈합육이 훨씬 심한 편이었다. Sodium dodecyl sulfate 화한 단백질을 polyacrylamide겔 전기영동함으로 분석한 결과, 보통육의 근원질단백질은 16개 성분, 그리고 혈합육의 근원질단백질은 12개 성분으로 구성되어 있었으며, 보장 10일째부터 보통육의 근원질단백질은에는 41,000dalton과 18,000dalton의 양분이 조금씩 증가하였고, 26,000 dalton과 23,500 dalton 및 23,000 dalton되 각 성분은 점차 감소하였다. 혈합육의 근원질단백질에 있어서는 49,000 dalton의 성분은 감소하였고 47.000 dalton의 성분은 새로이 형성되었으며, 26,000 dalton의 성분은 소감하였다. 근원섬유단백질의 전기영동분석결과에 의하면, 보통육의 근원섬유단백질은 17개 성분, 그리고 혈합육의 근원조직단백질은 16개의 성분으로 구성되어 있었다. 보장 10일에부터 보통육의 근원섬유단백질중에는 40,000 dalton의 성분이 증가하였고, 37,500 dalton의 성분은 점차 감소하였으며, 32,000 dalton의 성분은 새로히 출현하였다. 혈합육의 근원섬유단백질은 보장 9일째부터 58,000 dalton과 64,000 dalton의 성분은 그 농도가 단가하였으며, 17,500의 light chain-2 단백질은 소감하였고, 32,000 dalton의 성분은 새로이 출현하였다. 이 같은 전기영동상의 변화는 근원질단백질이 근원섬유단백질에 비하여 빨랐으며, 근원섬유단백질의 경화에 있어서는 혈합육쪽이 보통육에 비하여 빨랐다. 양 육의 단백질을 구성하는 아미노산을 분석한 결과, 즉살한 방어의 보통육 단백질은 글루탐산, 아스팔트산, 류신. 알기닌, 알라닌 등은 그 양이 어느 정도 많았고, 프롤린과 트?토판은 그 양이 적었으며, 혈합육에 있어서도 비슷한 경형이었다. 그리고 10일이 경과한 보통육에 있어서는 글루탐산과 아스팔트산이 현저히 감소하였으며, 9일이 경과한 혈합육에 있어서는 알라닌, 글리신, 그리고 알기닌이 현저히 감소하였다. 유리아미노산의 조성을 분석 결과, 즉살한 방어의 보통육중에는 히스티딘이 총유리아미노산의 약 $63\%$를, 그리고 혈합육중에는 타우린이 총유리아미노산의 약 $67\%$를 차지하는 양을 보였다. 그리고 $2^{\circ}C$에서 10일이 경과했을 때, 보통육에서는 히스티딘, 발린, 타우린이 증가하였으며, 알라닌, 류신 및 글리신 등은 조금 감소하였다. 같은 온도에서 9일이 경과한 혈합육에서는 타우린, 페닐알라닌, 글리신은 증하였으며, 히스티딘, 알라닌, 세린 등은 감소하였다.

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Thyroid Hormone-Induced Alterations of $Ca^{2+}-ATPase$ and Phospholamban Protein Expression in Cardiac Sarcoplasmic Reticulum

  • Kim, Hae-Won;Noh, Kyung-Min;Park, Mi-Young;Lee, Hee-Ran;Lee, Eun-Hee
    • The Korean Journal of Physiology and Pharmacology
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    • 제3권2호
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    • pp.223-230
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    • 1999
  • Alterations of cardiovascular function associated with various thyroid states have been studied. In hyperthyroidism left ventricular contractility and relaxation velocity were increased, whereas these parameters were decreased in hypothyroidism. The mechanisms for these changes have been suggested to include alterations in the expression and/or activity levels of various proteins; ${\alpha}-myosin$ heavy chain, ${\beta}-myosin$ heavy chain, ${\beta}-receptors,$ the guanine nucleotide-binding regulatory protein, and the sarcolemmal $Ca^{2+}-ATPase.$ All these cellular alterations may be associated with changes in the intracellular $Ca^{2+}$ concentration. The most important regulator of intracellular $Ca^{2+}$ concentration is the sarcoplasmic reticulum (SR), which serves as a $Ca^{2+}$ sink during relaxation and as a $Ca^{2+}$ source during contraction. The $Ca^{2+}-ATPase$ and phospholamban are the most important proteins in the SR membrane for muscle relaxation. The dephosphorylated phospholamban inhibits the SR $Ca^{2+}-ATPase$ through a direct interaction, and phosphorylation of phospholamban relieves the inhibition. In the present study, quantitative changes of $Ca^{2+}-ATPase$ and phospholamban expression and the functional consequences of these changes in various thyroid states were investigated. The effects of thyroid hormones on (1) SR $Ca^{2+}$ uptake, (2) phosphorylation levels of phospholamban, (3) SR $Ca^{2+}-ATPase$ and phospholamban protein levels, (4) phospholamban mRNA levels were examined. Our findings indicate that hyperthyroidism is associated with increases in $Ca^{2+}-ATPase$ and decreases in phospholamban levels whereas opposite changes in these proteins occur in hypothyroidism.

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