• YAKHAK HOEJI
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• v.34 no.5
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• pp.365-373
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• 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 $100\;{\mu}g/ml$.

• Korean Journal of Pharmacognosy
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• v.21 no.3
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• pp.210-216
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• 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.

• YAKHAK HOEJI
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• v.30 no.4
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• pp.174-179
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• 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.

• The Korean Journal of Zoology
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• v.8 no.2
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• pp.47-50
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• 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
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• v.3 no.3
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• pp.151-156
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• 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
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• v.33 no.3
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• pp.276-278
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• 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
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• v.49 no.3
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• pp.351-358
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• 2007

This experiment was conducted to determine correlation between in vitro protein fractions and in situ protein degradation rate with major dairy protein sources(soybean meal, corn gluten meal, cotton seed meal, kapok seed meal and perilla meal). Five protein fractions were obtained according to the Cornell Net Carbohydate and Protein System(CNCPS), and in situ protein degradation rates were determined by technique using nylon bags incubated for 0, 4, 8, 12 and 24hrs in the rumen of three Holstein steers. Fraction A was highest in kapok seed meal(14.6%) and lowest in corn gluten meal(0.6%) (P<0.05). The highest B1, B2 and B3 fractions were contained in soybean meal(8.27%), cotton seed meal(74%), and perilla meal(40%), respectively. Corn gluten meal was very high in fraction C. In situ protein degradation rate of soybean meal was 98%, highest among five protein sources, and corn gluten meal had the lowest rate at 28%. Correlation analysis showed that easily soluble fractions of both methods, in situ protein degradation rate and digestible protein fractions, and in situ protein degradation rate minus “a” and fraction B2+B3 were highly correlated. These results indicate that in vitro protein fractionation can be used in the estimation of in situ protein degradation.

• Journal of Life Science
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• v.8 no.1
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• pp.14-26
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• 1998

a- and c-raf protein kinase in the brain of rat, the protein pattern of cerebellum during postnatal development of rat by polyacryamide gel electrophoresis, and the existence of c-raf protein kinase by using Western blotting method. The results were as follows: The cytoplasm of Purkinje cells was, in general, strongly labeled with the antibodies of a- and c-raf protein kinases in the cortex regions such as Pyramis cerebelli, Unula, Nodulus, Paraflocculus, and Flocculus. C-raf protein kinase appeared stronger immunoreactivity than a-raf protein kinase. In peripheral of cytoplasm of Nucleus emboliformis, A-raf Protein kinase was labeled markedly. During postnatal development, the protein of 38,000 dalton increased gradually in the cytosolic fraction of cerebellum, and the protein of 260,600 dalton appeared in the membrane fraction of cerebellum. By immunoblotting method, the protein band of 74,000 dalton was detected in crude and cytosolic fractions, but it was not exhibited in membrane fraction, In this fact, it was identified that a - and c-raf proteins were distributed throughout neuronal cells, especially in the Purkinje cells, in normal cerebellum cortex of rat. Also, this phenomenon was assumed that raf protein kinase in cytoplasm of neuronal cell had to do with a certain functional mechanism and signal transduction of neurotransmitter as Protein kinase C.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.3
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• pp.364-370
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• 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
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• v.15 no.3
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• pp.167-170
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• 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.