• Title/Summary/Keyword: protein A

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Dietary Protein Restriction Alters Lipid Metabolism and Insulin Sensitivity in Rats

  • Kang, W.;Lee, M.S.;Baik, M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.24 no.9
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    • pp.1274-1281
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    • 2011
  • Dietary protein restriction affects lipid metabolism in rats. This study was performed to determine the effect of a low protein diet on hepatic lipid metabolism and insulin sensitivity in growing male rats. Growing rats were fed either a control 20% protein diet or an 8% low protein diet. Feeding a low protein diet for four weeks from 8 weeks of age induced a fatty liver. Expression of acetyl-CoA carboxylase, a key lipogenic enzyme, was increased in rats fed a low protein diet. Feeding a low protein diet decreased very low density lipoprotein (VLDL) secretion without statistical significance. Feeding a low protein diet down-regulated protein expression of microsomal triglyceride transfer protein, an important enzyme of VLDL secretion. Feeding a low protein diet increased serum adiponectin levels. We performed glucose tolerance test (GTT) and insulin tolerance test (ITT). Both GTT and ITT were increased in protein-restricted growing rats. Our results demonstrate that dietary protein restriction increases insulin sensitivity and that this could be due to low-protein diet-mediated metabolic adaptation. In addition, increased adiponectin levels may influences insulin sensitivity. In conclusion, dietary protein restriction induces a fatty liver. Both increased lipogenesis and decreased VLDL secretion has contributed to this metabolic changes. In addition, insulin resistance was not associated with fatty liver induced by protein restriction.

Protein A of Staphylococcus hyicus subsp hyicus isolated from pigs (돼지에서 분리한 Staphylococcus hyicus subsp hyicus의 protein A)

  • Kim, Do-kyoung;Yeo, Sang-geon
    • Korean Journal of Veterinary Research
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    • v.30 no.2
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    • pp.187-192
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    • 1990
  • The Presence and quantity of protein A in Staphylococcus hyicus subsp hyicus isolates from pigs were determined by indirect hemagglutination test and enzyme-linked immunosorbent assay(ELISA). Cell-bound and extracellular protein A was demonstrated in 87.7% and 36.0% of 489 isolates, respectively, by indirect hemagglutination test. When contents of the protein A were estimated by ELISA method, all of the isolates that were positive to protein A in indirect hemagglutination test produced extracellular protein A of less than 1ng/ml. Most of the isolates produced cell-bound protein A of less than 1ng/ml, whereas 28 isolates produced 1 to 35ng/ml and 11 isolates produced 25 to 108ng/ml.

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Immunocytochemical Localization Qf raf Protein Kinase in Cerebrum of Geoclemys reevesii (Gray) (남생이(Geoclemys reevesii) 대뇌에 있어서 raf Protein Kinase의 면역세포화학적 분포)

  • 최원철;문현근
    • The Korean Journal of Zoology
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    • v.33 no.2
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    • pp.141-151
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    • 1990
  • Raf protein kinases and protein kinase C belong to serine/threonine-specific proteins in the cytoplasin, and are similar to each other in functional structure and the aspect of the distribution of celI. The distribution of raf protein kinase in the cerebrum of Geoclemys reevesfi as studied by using the antibodies against a-raf and c-raf protein kinase which induce the expression of raf fainily oncogenes. In general, raf protein kinases were distributed in such restricted regions as the general pallium, hippocampal formation, pdmordiuin hippocampi,nucleus of lateral olfactory tract, basal amygdaloid nucleus, and bed of stria terminalis. Immunological labeling of c-raf protein kinase was more widespread than that of a-raf. However, the intensity of the labeling of c-raf was lower than that of a-raf. The spherical cells of basal amygdaloid nucleus is a ring-like form, because only the cytoplasm was imunolabeled. Especially, c-raf protein kinase occurred in the cells which contained protein kinase C abundandy such as pyramidal cells and Purkinje cells. This suggests that a- and e-raf protein kinases may synegistically induce carclnoma with myc gene which is activated by protein kinase C.

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Simulation of the Effect of Protein Quality at the Different Protein Intake Level on Protein Metabolism (각기 다른 단백질섭취 수준에서 본 식이단백질의 질이 단백질대사에 미치는 영향 -Simulation Model을 이용하여-)

  • 이옥희
    • Journal of Nutrition and Health
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    • v.26 no.9
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    • pp.1033-1048
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    • 1993
  • This study was designed to describe the effect of the protein quality at different intake level of protein on the protein metabolism in the whole body of growing pigs with a simulation model. Varying to the protein level in feeds, four simulations were conducted. The feed protein level, represented as proportions of digestible protein to the metabolic energy (DP/ME, g/MJ), were 6-8, 11-13, 17-19, and 23-25 DP/ME, respectively. Two protein quality and six weeks of growth time were used at each simulation. The objective function for the simulations was protein deposition in the whole body, which was calculated from the experimental results. The parameters in the simulation were determined by the parameter estimation technique. The results obtained from the simulation were as follows: The protein synthesis and breakdown rates(g/day) in the whole body was increased with the increase of protein quality only at lower or required level of protein intake. They showed a parallel behavior in the course of growth, irrespective of quality and level of feed protein intake. The simulated protein deposition and protein synthesis showed a linear relationship between them at different protein quality and level. The affinity parameter showed a linear relationship between them at different protein quality and level. The affinity parameter showed that arginine, tryptophan and isoleucine were more efficient in the stimulation ofbody protein synthesis. Lysine and phenylalanine+tyrosine were less efficient. The oxidation parameter showed that histidine, pheyalanine+tyrosine were less efficient. The oxidation parameter showed that histidine, phenyalanine+tyrosine, and methionine+cystine were oxidized in larger magnitude than lysine and threonine. The oxidation parameter of most amino acids increased with the increase of protein intake beyond the requirement level, but not any more at highest protein intake level. Finally it was found that the improvement of feed protein quality at the lower or required level of protein intake increase protein deposition through a parallel increase of protein synthesis and breakdown.

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A Simulation Model for the protein Deposition of Pigs According to Amino Acid Composition of Feed Proteins (사료의 아미노산 조성에 따른 돼지의 단백질 축적을 나타내는 수치모델)

  • 이옥희;김강성
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.28 no.1
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    • pp.178-190
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    • 1999
  • This study was conducted to develop a simulation model for the growth dynamics of pigs and to describe quantitatively protein deposition depending on the amino acid composition of feed protein. In the model it is assumed that the essential processes that determine the utilization of feed protein in the whole body are protein synthesis, breakdown of protein, and oxidation of amino acid. Besides, it is also assumed that occurrence of protein deposition depends on genetic potential and amino acid composition of feed protein. The genetic potential for the protein deposition is the maximum capacity of protein synthesis, being dependent on the protein mass of the whole body. To describe the effect of amino acid composition of feed on the protein deposition, a factor, which consist of ten amino acid functions and lie between 0 and 1, is introduced. Accordingly a model was developed, which is described with 15 flux equations and 11 differential equations and is composed of two compartments. The model describes non linear structure of the protein utilization system of an organism, which is in non steady state. The objective function for the simulation was protein deposition(g/day) cal culated according to the empirical model, PAF(product of amino acid functions) of Menke. The mean of relative difference between the simulated protein deposition and PAF calculated values, lied in a range of 11.8%. The simulated protein synthesis and breakdown rates(g/day) in the whole body showed a parallel behavior in the course of growth.

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A new purification method for the Fab and F(ab)2 fragment of 145-2C11, hamster anti-mouse CD3ε antibody

  • Kwack, Kyu-Bum
    • BMB Reports
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    • v.33 no.2
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    • pp.188-192
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    • 2000
  • Recombinant protein G has been utilized in the purification of antibodies from various mammalian species based on the interaction of antibodies with protein G. The interaction between immunoglobulin and protein G may not be restricted to the Fc protion of antibodies, as many different $F(ab)_2$ or Fab fragments can also bind to protein G. I found both FAb $F(ab)_2$ of 145-2C11, a hamster anti-mouse $CD3{\varepsilon}$ antibody, bound to the protein G-sepharose. Interestingly, Fab and $F(ab)_2$ of 145-2C11 did not bind to the protein A-sepharose. The binding of Fab and $F(ab)_2$ of 145-2C11 to protein G provided a useful method to remove proteases, chopped fragments of the Fc region, and other contaminating proteins. The remaining intact antibody in the protease reaction mixture can be removed by using a protein A-sepharose, because the Fab and $F(ab)_2$ portions of 145-2C11 did not bind to protein A-sepharose. The specific binding of Fab and $F(ab)_2$ portions of 145-sC11 to a protein G-sepharose (though not to a protein A-sepharose) and binding of intact 145-2C11 to both protein A- and G-sepharose will be useful in developing an effective purification protocol for Fab and $F(ab)_2$ portions of 145-2C11.

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Analysis of Double Stranded DNA-dependent Activities of Deinococcus radiodurans RecA Protein

  • Kim, Jong-Il
    • Journal of Microbiology
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    • v.44 no.5
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    • pp.508-514
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    • 2006
  • In this study, the double-stranded DNA-dependent activities of Deinococcus radiodurans RecA protein (Dr RecA) were characterized. The interactions of the Dr RecA protein with double-stranded DNA were determined, especially dsDNA-dependent ATP hydrolysis by the Dr RecA protein and the DNA strand exchange reaction, in which multiple branch points exist on a single RecA protein-DNA complex. A nucleotide cofactor (ATP or dATP ) was required for the Dr RecA protein binding to duplex DNA. In the presence of dATP, the nucleation step in the binding process occurred more rapidly than in the presence of ATP. Salts inhibited the binding of the Dr RecA protein to double-stranded DNA. Double-stranded DNA-dependent ATPase activities showed a different sensitivity to anion species. Glutamate had only a minimal effect on the double-stranded DNA-dependent ATPase activities, up to a concentration of 0.7 M. In the competition experiment for Dr RecA protein binding, the Dr RecA protein manifested a higher affinity to double-stranded DNA than was observed for single-stranded DNA.

Critical Review on an Effect of Dietary Protein Content on the Xenobiotics Metabolism in Rats (식이성 단백질 함량이 Xenobiotics 대사에 미치는 영향)

  • 윤종국
    • Journal of the East Asian Society of Dietary Life
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    • v.5 no.3
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    • pp.385-394
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    • 1995
  • Our previous reports on the effect of dietary protein on methanethiol, ethacrynic acid, bromobenzene and carbon tetrachloride metabolism were overall reviewed. The methanethiol, ethacrynicacid and bromobenzene treated rats showed the more severe liver damage in those fed a low protein diet than those fed a standard protein diet. These xenobiotics treated rats showed the lower content of hepatic glutathione and its conjugated enzyme, glutathione S-transferase activities in those fed a low protein diet than those fed a standard protein diet. In case of carbon tetrachloride treated rats, the liver damage was more reduced in rats fed a low protein diet than those fed a standard protein diet. Concomitantly the hepatic cytochrome P-450 content, and its decreasing rate to the control were lower in rats fed a low protein diet than those fed a standard protein diet.

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Effects of an Anabolic Steroid, Nandrolone Phenylpropionate, on Reductions in Body and Muscle Proteins Under the Dietary Regimens of Feeding a Low-Protein Diet and of 50% Food Restriction in Rats

  • Choo, Jong-Jae
    • Nutritional Sciences
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    • v.1 no.1
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    • pp.3-7
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    • 1998
  • The aim of the present investigation was to see whether an anabolic steroid, nandrolone phenylpropionate (NPP), exerts protienanabolic effects under such adverse nutritional conditions as protein deficiency and protein-energy malnutrition in male rats. feeding on a low-protein (8% casein) diet resulted in a marked reduction in body weight gain that was associated with reductions in body protein and protein content of gastrocnemius muscle. Administration of NPP (4 mg/kg body weight) did not alter muscle and body protein depletion induced by a low-protein diet. 50% food restriction caused reductions in body protein and in protein content of gastrocnemius muscle. These reductions were partially prevented by NPP (4 mg/kg body weight). Food restriction did not affect plasma concentration of corticosterone, insulin, or tetosterone plus dihydrotestosterone. On the other hand, neither plasma concentration of corticosterone nor insulin were affected by NPP. The present results show that anabolic steroids do not express anabolic effects under conditions of protein deficiency, but in protein-energy malnutrition, anabolic steroids exert their anabolic effects even in male rats.

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Salt-Induced Protein Precipitation in Aqueous Solution: Single and Binary Protein Systems

  • Kim, Sang-Gon;Bae, Young-Chan
    • Macromolecular Research
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    • v.11 no.1
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    • pp.53-61
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    • 2003
  • A molecular-thermodynamic model is developed for the salt-induced protein precipitation. The protein molecules interact through four intermolecular potentials. An equation of state is derived based on the statistical mechanical perturbation theory with the modified Chiew's equation for the fluid phase, Young's equation for the solid phase as the reference system and a perturbation based on the protein-protein effective two body potential. The equation of state provides an expression for the chemical potential of the protein. In a single protein system, the phase separation is represented by fluid-fluid equilibria. The precipitation behaviors are simulated with the partition coefficient at various salt concentrations and degree of pre-aggregation effect for the protein particles. In a binary protein system, we regard the system as a fluid-solid phase equilibrium. At equilibrium, we compute the reduced osmotic pressure-composition diagram in the diverse protein size difference and salt concentrations.