• Archives of Pharmacal Research
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• 제19권6호
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• pp.502-506
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• 1996

Protein X is one of the subunits of pyruvate dehydrogenase complex. The biological role of this protein has not been fully elucidated, mainly because of the difficulty in its dissociation from the tightly bound dihydrolipoamide acetyltransferase-protein X subcomplex. We have found that the detachment of protein X from acetyltransferase subunit can be easily accomplished by the cycles of freezing and thawing proces. Several lines of evidence including sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequence analysis and acetylation with $[2^{14}C]$ pyruvate confirmed that the purified protein is protein X. The purified intact form of protein X was acetylated by $[2^{14}C]$ pyruvate in the presence of py-ruvate dehydrogenase subunit.The acetylation efficiency of this protein was lower than that of acetyltransferase and was not affected by the presence of acetyltransferase.

• Bulletin of the Korean Chemical Society
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• 제25권11호
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• pp.1676-1680
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• 2004

We demonstrate that wide-angle X-ray scattering pattern from photoactive yellow protein (PYP) in solution using a high flux third generation synchrotron X-ray source reflects not only the overall structure, but also fine structures of the protein. X-ray scattering data from PYP in solution have been collected in q ranges from 0.02 ${\AA}^{-1}$ to 2.8 ${\AA}^{-1}$. These data are sensitive to the protein structure and consistent with the calculation based on known crystallographic atomic coordinates. Theoretical scattering patterns were also calculated for the intermediates during the photocycle of PYP to estimate the feasibility of time-resolved wide-angle X-ray scattering experiments on such proteins. These results demonstrate the possibility of using the wide-angle solution X-ray scattering as a quantitative monitor of photo-induced structural changes in PYP.

• 한국가금학회지
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• 제12권1호
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• pp.39-44
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• 1985

본 조사연구는 계란의 중량등급별 영양가를 조사하고 적정가격을 검토하기 위하여 600개의 계란을 공시하여 계란의 중량등급별 평균란중, 란황과 란백 및 란각의 구성비, 란황과 란백의 영양성분 분석, 계란의 단백질과 지방함량 조사를 실시하고, 계란의 란중과 단백질함량 및 단백질＋지방함량을 기준으로 하는 적정가격을 검토하였는 바 얻어진 결과는 다음과 같다. 1. 평균란중(X, g/10개)의 증가에 따라 란황의 비율(Y, %)은 Y=44.34-0.02X로 감소하고, 란백의 비율(Y, %)은 Y=40.136＋0.026X로 증가하였으며, 란각의 비율(Y, %)은 Y=15.358-0.006X로 감소하였다. 2. 란황과 란백의 영양분석은 계란의 중량에 따라 큰 차이나 일정한 경향을 보이지 않았다. 3. 평균란중(X, g/10개)의 증가에 따라 전란의 단백질함량(Y, %)은 Y=11.943-0.00032X로 감소하고, 지방함량(Y, %)은 Y=13.996-0.00614X로 역시 감소하였으며, 단백질＋지방함량(Y, %)는 Y=25.939-0.00646X로 감소하였다. 4. 평균란중을 기준으로 하는 적정가는 단백질함량을 기준으로 하는 적정가와 비슷한 경향을 보였으며, 이들 적정가는 단백질＋지방함량을 기준으로 하는 적정가보다 특란과 왕란에서는 높게 그리고 경란-중란에서는 낮게 평가되었으며, 시가와 비교할 때 단백질＋지방함량기준 적정가가 가장 비슷한 경향을 보였다.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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• pp.260-260
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• 1994

Mammalian pyruvate dehydrogenase complex(PDC) enzyme consists of multiple oopies of three major oligomeric enzymes-El, E2 E3. And protein X is one of the enzymatic constituents which is tightly bound to E2 subunit This complex enzyme is responsible for the oxidative decarboxylation of pyruvate producing of acetyl CoA which is a key intermediate for the entry of carbohydrates into the TCA cycle for its complete metabolic conversion to CO$_2$. And the overall activity of the complex enzyme is regulated via covalent nodification of El subunit by a El specific phosphatase ad kinase. Protein X has lipoyl moiety that undergoes reduction and acetylation during ezymatic reaction and has been known h be involved in the binding of E3 subunit to E2 core and in the regulatory activity of kinase. The purification of protein X has not been achieved majorly because of its tight binding to E2 subunit The E2-protein X subcomplex was obtained by the established methods and the detachment of protein X from E2 was accomplished in the 0.1M borate buffer containing 150mM NaCl. During the storage of the subcomplex in frozen state at -70$^{\circ}C$, the E2 subunit was precipitated and the dissociated protein X was obtained by cntrifegation into the supernatant The verification of protein X was accomplished by (1)the migration on SDS-PAGE, (2)acetylation by 〔2$\^$-l4/C〕 pyruvate, and (3)internal amino acid sequence analysis of tryptic digested enzyme.

• 대한의생명과학회지
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• 제2권1호
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• pp.127-132
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• 1996

한국인 일반 정신박약자들의 핵형 및 혈청단백질을 분석한 결과는 다음과 같다. 정신박약자 35명 중 3명에서 fragile X 염색체를 발견하였고 그 빈도는 4~l5%였다. Fragile X 증후군 환자들의 혈청단백질의 농도는 5.73$\pm$0.89(g/ dl) 이었고 albumin과 globulin의 비는 0.86$\pm$0.14 이었다. 일반 정신박약자들의 혈청단백질 농도는 6.83$\pm$0.72(g/dl) 이었고 이중 albumin과 globulin의 비는0.87$\pm$0.47 이었다. Fragile X증후군환자 및 일반정신박약자들의 혈청단백질 농도 및 albumin과 globulin의 비는 정상인 및 Down 증후군환자들 보다 낮았다.

• 한국동물학회지
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• 제26권3호
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• pp.181-192
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• 1983

이차원 전긱영동법에 의하여 A. proteus의 tD strain과 tD strain이 박테리아와 공생에 의해 유도된 xD strain의 단백질 양성을 비교하였다. Silver stain에 의해 비교 가능한 200여개의 주요 단백질 가운데 tD strain에서 분자량 45,000, 동전점 5.9의 특이성 단백질이, xD strain의 세포액과 공생낭에서는 분자량 29,000, 동전점 5.5의 공생 특이성 단백질이 탐지되었다. 공생 특이성 단백질은 아메바 고은 배양 및 실험 공생 아메바를 이용한 실험 결과 박테리아와 직접 연관 되어 있었다. 탐지된 두 특이성 단백질에 대하여 종전의 세포 핵 이식 및 배양 실험을 통해서 얻어진 결과에 비추어 이들 단백질 상호 연관 및 세포내의 기능에 관하여 논의하였다.

• Environmental Engineering Research
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• 제20권2호
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• pp.163-169
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• 2015

In this study, we attempted to solubilize protein in slaughter blood (SB) using ultrasonic technology. The application of ultrasonic technology can make enzymatic degradation of SB more effective, which has no comparable alternative for treatment. The SB was homogenized by grinding it for 10 minutes at 10,000 rpm as a pretreatment for preventing its clotting, and then ultrasonic treatment was attempted to solubilize protein in SB. To maximize the efficiency of ultrasonic treatment for SB, the optimum condition of ultrasonic frequency (UF) was determined to be 20 kHz. To optimize the operation conditions of ultrasonification with 20 kHz of frequency, we used response surface methodology (RSM) based on ultrasonic density (UD) and ultrasonification time (UT). The solubilization rate (SR) of protein (%) was calculated to be $101.304-19.4205X_1+0.0398X_2+7.9411X_1{^2}+0.0001X_2{^2}+0.0455X_1X_2$. From the results of the RSM study, the optimum conditions of UD and UT were determined at 0.5 W/mL and 22 minutes, respectively, and SB treated under these conditions was estimated to have a 95% SR. Also, experimentally, a 95.53% SR was observed under same conditions, accurately reflecting the theoretical prediction of 95%.

• Molecules and Cells
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• 제28권6호
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• pp.501-507
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• 2009

Fragile X syndrome (FXS) is caused by a lack of the fragile X mental retardation protein (FMRP) due to silencing of the Fmr1 gene. As an RNA binding protein, FMRP is thought to contribute to synaptic plasticity by regulating plasticity-related protein synthesis and other signaling pathways. Previous studies have mostly focused on the roles of FMRP within the hippocampus - a key structure for spatial memory. However, recent studies indicate that FMRP may have a more general contribution to brain functions, including synaptic plasticity and modulation within the prefrontal cortex. In this brief review, we will focus on recent studies reported in the prefrontal cortex, including the anterior cingulate cortex (ACC). We hypothesize that alterations in ACC-related plasticity and synaptic modulation may contribute to various forms of cognitive deficits associated with FXS.

• 한국식품과학회지
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• 제29권4호
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• pp.752-757
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• 1997

Papaya 유액 추출물에서 protein을 정제 회수하기 위해 papaya 유액으로부터 추출한 추출액을 경제적이고도 처리가 비교적 간단한 ethanol 침전방법을 사용하였다. 실험계획법에 의하여 설정된 3수준의 부분요인 실험법에 의하여 실시된 각 처리구의 실험 결과를 다중 회귀분석 방법에 의해 다음과 같은 모델식 $Y=7.4554+1.2657X_{2}+1.0552X_{3}-1.7407X_{4}-0.01666X_{2}\;^{2}-0.1134X_{4}^{2}$을 산출하였으며 pH는 다중 회귀분석에 의해 제거되었다. 반응표면 분석법(RSM)을 이용한 결과 protein을 회수하기 위한 최적 조건으로는 protein 농도가 38.2 mg/ml, 40%의 ethanol 농도, 침전 온도는 $-8^{\circ}C$였다. 이러한 최적 조건에 의한 회수율의 실험치는 68.97%로 예측치인 77.28%에 근접한 결과였다. 또한 유의 수준을 검정하는 자유도와 F-value도 양호한 값(p<0.001)을 나타내어 종속변수와 독립변수와의 상관관계가 뛰어남을 알 수 있으며 따라서 다중 회귀분석에 얻어진 모델식의 각 변수들 사이에는 유의성이 높음을 알 수 있었다.

• 한국수산과학회지
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• 제35권4호
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• pp.451-453
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• 2002

The rotation of the flagellar motor is powered by the electrochemical gradient of specific ions across the cytoplasmic membrane. Recently, the gents of the Na'-driven motor have been cloned from marine bacterium of Vibrio sp. and some of the motor proteins have been purified and characterized. Also, motx gene encoding a channel component of the sodium type flagellar motor was identified from Vibrio Huuiaiis (KTCC 2473). The amino acid sequence of MotX protein from V, Huvialis shared 90, 85, $85\%$ identity with V, cholerae, V. alginolyticus, V parahaemolyticus, respectively. We have studied the localization of the expressed MotX protein in Escherichia coli by immune-gold labeling of ultra-thin frozen section. Our observation of the expressed protein indicated that MotX protein could be existed as attachment to inner membrane in E. coli.