• 약학회지
• /
• 제34권5호
• /
• pp.365-373
• /
• 1990

The effects of the protein fraction of Panax ginseng on primary cultured chicken embryonic brain cells and DRG cultured with a deficient medium were studied. The protein fraction was further fractionated into four groups according to the molecular weight; larger than 10,000 dalton(fraction A), between 5,000 and 10,000 daltons(fraction B), between 1,000 and 5,000 daltons(fraction C), between 500 and 1,000 daltons(fraction D). All four protein fractions at the concentration of $100\;{\mu}g/ml$ significantly increased the number of the brain cells which promoted the neurite outgrowth. The activity of PDHC in the brain cells was elevated significantly by the protein fraction B at the concentration of $100\;{\mu}g/ml$. It was noted that $100\;{\mu}g/ml$ protein fraction C and D significantly enhanced the synthesis of protein in the brain cells. At the concentration of $100\;{\mu}g/ml$, the protein fraction B enhanced RNA synthesis and the protein fraction A significantly enhanced DNA synthesis in the brain cells. The protein fractions B, C, and D significantly promoted the neurite outgrowth of DRG at the concentration of $100\;{\mu}g/ml$.

• 생약학회지
• /
• 제21권3호
• /
• pp.210-216
• /
• 1990

Effects of the protein fraction of Panax ginseng on chicken embryonic skeletal muscle cells cultured with a decfiient medium were studied. The protein fraction was further fractionated into four groups according to the molecular weight; larger than 10,000 dalton(fraction A), between 5,000 and 10,000 dalton(fraction B), between 1,000 and 5,000 dalton(fraction C), between 500 and 1,000 dalton(fraction D). According to the microscopic observation, all four protein fractions at the concentration of $10{\sim}100{\;}{\mu}g/ml$ showed the tendency to stimulate the growth and differentiation of the muscle cells. The activity of acetylcholinesterase in muscle cells was significantly elevated by the protein fraction A at the concentration of $100{\mu}{\;}g/ml$. Protein fractions B,C and D significantly enhanced the synthesis of RNA in the muscle cells. The synthesis of DNA in muscle cells was significantly enhanced by protein fractions A,B and C.

• 약학회지
• /
• 제30권4호
• /
• pp.174-179
• /
• 1986

The thymus weight of the mouse was 54.1% in protein malnutritive diet group and 39.2% in group treated with saponin fraction of Panax ginseng in comparison to normal diet group. This decreasing effects of protein malnutritive diet and saponin fraction on the thymus weight practically disappeared after four weeks. The saponin fraction showed no effect on the spleen weight of the mouse. The supplement of the saponin fraction enhanced total peritoneal exudate cells, content of total serum protein and albumin content of the mouse, each 45, 8 and 10% respectively in comparision to that of normal diet group. And these values in protein malnutritive diet group were 61.2, 83.6 and 87.0% respectively in comparision to that of normal diet group, and recovered to the level of normal diet group by the supplement of the saponin fraction. The electrophoregram of the serum protein of the mouse fed with protein malnutritive diet was different from that of the mouse fed with normal diet, but this difference practically disappeared by the supplement of the saponin fraction.

• 한국동물학회지
• /
• 제8권2호
• /
• pp.47-50
• /
• 1965

양서류 오종 Bombina orientalis , Cacopoides borealis , Bufo bufo asiaticus, Rana nigromaculata nigromaculata, Rana rugosa 의 혈청단백질을 Paper electrophoresis 의 방법으로 분석비교하였다. 그 결과 Bombina orientalis 의 혈청단백질은 인간의 것과 마찬가지로 5개의 protein fraction으로 나누어지고 그중 fraction III 단백지링 가장 많은 함량을 구성하며 peak 가 가장 높다. Cacopoides borealis 와 Bufo bufo asiaticus 의 혈청단백질은 4개의 protein fraction 으로 나누어지는데 Cacopoides boreealis 에서는 fraction IV protein이 Bufo bufo asiaticus 에서는 fraction I protein 이 가장 많은 함량을 구성하고 있다. Rana nigromaculata nigromacuata 와 Rana rugosa 는 graph 상에 나타난 peak로 보면 상호유사하나 protein fraction 수는 차이가 있다. 그리고 albumin은 전 함량 per centage의 약 반을 차지하고 있다. 즉 종간의 거리가 멀수록 protein fraction 의 차이가 percentage 함량에 있어서 명백하여짐을 암시하여준다.

• Advances in Traditional Medicine
• /
• 제3권3호
• /
• pp.151-156
• /
• 2003

The leaves of Mirabilis jalapa L contains protein fraction presumed ribosome-inactivating protein (RIP). RIP is a group of protein that has RNA N-glycosidase activity that is capable to inhibit protein synthesis. Protein fraction of the plant was shown to be cytotoxic on HeLa cell-line, however, the mechanism by which the protein kill the cells is not identified yet, whether trough apoptosis, necrosis, or other mechanism. This research aim to study the mechanism of cell death caused by the protein fraction isolated from the leaves of this plant on HeLa and Raji cell-line, as representative of different kind of cancer cells. Results showed that protein fraction isolated from the leaves of Mirabilis jalapa L was more cytotoxic to HeLa cell-line (LC50: 0.65 mg/ml) than to Raji cell-line (1.815 mg/ml) on 48 hours incubation time. Moreover, it was demonstrated that the death of HeLa cells caused by the protein fraction was due to induction of apoptosis, while on Raji cell-line was due to non-apoptosis way, presumably via necrosis.

• BMB Reports
• /
• 제33권3호
• /
• pp.276-278
• /
• 2000

The postsynaptic density (PSD), a large protein complex beneath the postsynaptic membrane, is notorious for its 'stickiness'. In order to understand the molecular composition of the PSD fraction, a 17 kDa protein band was isolated by electroelution from SDS-geis, and its partial amino acid sequence was determined from HPLC-purified tryptic peptides of the protein. Surprisingly, the amino acid sequence was identical to that of the previously reported 17 kDa isoform of the myelin basic protein (MBP), an essential protein in CNS myelin formation. Since the protein band represented ~2% of the total proteins in the 1 % n-octyl glucoside-insoluble PSD fraction, these results indicate that a significant amount of the 17 kDa isoform of MBP is tightly associated with the PSD during preparation of the PSD fraction.

• Journal of Animal Science and Technology
• /
• 제49권3호
• /
• pp.351-358
• /
• 2007

본 연구는 국내에서 사용되고 있는 몇 가지 단백질 원료사료를 사용하여 단백질 fraction과 in situ 단백질 분해율을 구한 다음 이들 사이에서의 상관관계를 살펴보고자 실시하였다. 원료사료는 대두박, 콘글루텐, 면실박, 카폭박 및 임자박이었다. 단백질 fraction은 CNCPS에서 제시하는 방법으로 구하였으며, in situ 단백질 분해율은 캐뉼라가 장착된 홀스타인 거세우 3두를 이용하여 반추위에서 원료사료를 4, 8, 12 및 24시간 배양하여 구하였다. 단백질 fraction 중 A fraction은 카폭박이 14.6%로 가장 높았고, 콘글루텐이 0.6%로 가장 낮았다(P<0.05). B1 fraction은 대두박이 8.27%로 가장 높았으며, B2 fraction은 대두박과 면실박이 74%로 가장 높았다. B3 fraction은 임자박이 40%로 다른 원료사료에 비교해 뚜렷하게 높았다. C fraction은 콘글루텐이 약 42.5%로 가장 높았다. In situ 조단백질 분해율은 대두박이 98%로 가장 높았고, 콘글루텐은 28%로 가장 낮았다. 단백질 fraction과 in situ 분해율 사이의 상관관계를 보면, 쉽게 용해되는 부분(A, B1 fraction vs a값) 사이에, in situ 조단백질 분해율과 소화가능한 단백질 fraction 사이에, 그리고 in situ 조단백질 분해율에서 a값을 제외한 값과 B2+B3 fraction 사이에는 상관관계가 높았다(P<0.01). 본 연구결과에 의하면, 단백질 fraction은 원료사료의 반추위내 분해율을 추정하는 데 이용될 수 있을 것으로 사료되며, 앞으로 더 정확한 평가를 위해서는 더 많은 원료사료에 대한 분석이 필요하다고 본다.

• 생명과학회지
• /
• 제8권1호
• /
• pp.14-26
• /
• 1998

본 연구에서는 SDS/polyacrylamide 젤 전기영동에 의한 쥐의 성장과정에 따른 소뇌의 단백질양상의 변화양상과 immunocytochemistry를 이용하여 c-raf a-raf kinase의 정상 소뇌에서의 분포에 대해 관찰 하였으며 western blot을 이용하여 소뇌의 단백질들에서 c-raf의 존재에 대해 살펴보았다. 단백질 양상에서 쥐의 성장에 따라 crude에선,ㄴ 49,200 dalton과 169,000 dalton 사이의 bands가 양적 증가를 보였으며 cytosolic fraction 에서는 37,800 dalton의 band가 양적 증가를 보이는데 비해 membrane fraction 에서는 260,600 dalton의 band가 증가하였다. 이러한 결과로 성장 발달에 따라 고분자 량의 물질들이 이들 소뇌 부위에서 기여하였을 것으로 추정할 수 있었다. Immunocytochemistry에 의한 분석에서는 c-raf와 a-raf가 소뇌의 피질주위에서 조롱박 세포(Purkinje cell) 의 세포질 특히 핵 주변부위에서 강하게 검출되었으며 a-raf에 비해 c-raf가 더 강하게 나타났었다. 그리고 그 외에 Nucleus embolifornis의 큰 neuronal cell의 세포질 부위의 나타남을 볼 수 있었다. Immunoblot에 의한 분석에서는 crude와 cytosolic fraction에서 raf protein kinase의 존재를 확인할 수 있었으며, 이상의 결과들을 종합해 보았을 때 소뇌의 정상의 많은 신경세포(neuronal cell)에 raf protein kinase가 분포되어 있으며 이들이 정상의 cell에서 기능을 가질 것으로 추정된다.

• Asian-Australasian Journal of Animal Sciences
• /
• 제21권3호
• /
• pp.364-370
• /
• 2008

Chemical analysis and in vitro studies were conducted to investigate the nutritive value for ruminants of cell mass from lysine production (CMLP) which is a by-product of the lysine manufacturing process. Proximate analysis, protein fractionation, and in vitro protein degradation using protease from Streptomyces griseus and strained ruminal fluid were carried out to estimate ruminal protein degradability of CMLP with two reference feedstuffs-soybean meal (SBM) and fish meal (FM). Amino acid composition and pepsin-HCl degradability were also determined to evaluate postruminal availability. CMLP contained 67.8% crude protein with a major portion being soluble form (45.4% CP) which was composed of mainly ammonium nitrogen (81.8% soluble CP). The amount of nucleic acids was low (1.15% DM). The total amount of amino acids contained in CMLP was 40.60% DM, which was lower than SBM (47.69% DM) or FM (54.08% DM). CMLP was composed of mainly fraction A and fraction B2, while the protein fraction in SBM was mostly B2 and FM contained high proportions of B2 and B3 fractions. The proportion of B3 fraction, slowly degradable protein, in CP was the highest in fish meal (23.34%), followed by CMLP (7.68%) and SBM (1.46%). CMLP was degraded up to 51.40% at 18 h of incubation with Streptomyces protease, which was low compared to FM (55.23%) and SBM (83.01%). This may be due to the insoluble portion of CMLP protein being hardly degradable by the protease. The in vitro fermentation by strained ruminal fluid showed that the amount of soluble fraction was larger in CMLP (40.6%) than in SBM (17.8%). However, because the degradation rate constant of the potentially degradable fraction of CMLP (2.0%/h) was lower than that of SBM (5.8%/h), the effective ruminal protein degradability of CMLP (46.95%) was slightly lower than SBM (53.77%). Unavailable fraction in the rumen was higher in CMLP (34.0%) compared to SBM (8.8%). In vitro CP degradability of CMLP by pepsin was 80.37%, which was lower than SBM (94.42%) and FM (89.04%). The evaluation of protein degradability using different approaches indicated that soluble protein in CMLP may supply a large amount of ammonia in the rumen while insoluble protein can be by-passed from microbial attacks due to its low degradability. The results from this study suggest that CMLP can be used as a protein supplement to ruminants for supplying both non-protein nitrogen to rumen microbes and rumen undegradable protein to the host animal.

• Journal of Ginseng Research
• /
• 제15권3호
• /
• pp.167-170
• /
• 1991

Radiation protective fraction was Isolated and partially purified from Korean white ginseng. The effect of the fraction was studied on the cell survival of W-damaged CHO-Kl cells. As a result, it was found that the fraction increased the survival rate of damaged cells significantly within the dose range of which cytotoxicity did not appear This fraction was separated into two parts by adding butanol, namely the precipitated protein component and the butanol extract. Damaged cells were treated with each of these components and their survival rates were measured. The protein component demonstrated significant increase in the survival rates, while the butanol extract showed no such increment. These results suggest that the radiation protective effect of the ginseng fraction is originated from the butanol-precipitated protein component, not from the butanol-soluble compounds.