• Journal of Photoscience
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• 제9권2호
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• pp.335-337
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• 2002

Blue light (BL) induces stomatal opening through activation of H$^{+}$ pump, which creates electrical gradient across the plasma membrane for $K^{+}$ uptake into guard cells. The pump is the plasma membrane H$^{+}$ -ATPase and is activated via phosphorylation of the C-terminus with concomitant binding of the 14-3-3 protein. The opening is initiated by the perception of BL through phototropin (phot), which are recently identified as BL receptors in stomatal guard cells. In this study, we provide the biochemical evidence for phots as BL receptors in stomatal guard cells. vfphot was phosphorylated reversibly by BL, and phosphorylation levels of vfphot increased earlier than those of the plasma membrane W-ATPase. BL-dependent phosphorylations of vfphot and H$^{+}$-ATPase showed similar fluence dependency. Staurosporin, an inhibitor of serine/threonine protein kinase, and diphenyleneiodonium chloride (DPI), an inhibitor of flavoprotein, inhibited BL-dependent phosphorylations of vfphot and H$^{+}$ -ATPase. These results indicate that vfphot acts as a BL-receptor mediating stomatal opening.l opening.

• Macromolecular Research
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• 제11권6호
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• pp.451-457
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• 2003

Anion-substituted poly(vinyl alcohol) (PVA) membranes, carboxymethylated PVA (C-PVA), and sulfonated PVA (S-PVA) were prepared and the effects of these substitutions on the plasma protein adsorption were studied by one- and two-dimensional gel electrophoresis and immunoblotting. When Cuprophane was used as a negative control, the amount of total proteins bound to samples decreased in the order Cuprophane > PVA > C-PVA > S-PVA, which we attribute to the effects of the surface characteristics of the samples, such as their surface tensions and electrostatic properties, on the adsorption of proteins to the surfaces of the materials. The results revealed that albumin was the most abundant protein in all the samples. The proportion of adsorbed fibrinogen to S-PVA exceeded those of PVA and C-PVA, whereas S-PVA exhibited the lowest IgG adsorption affinity among the samples we studied.

• BMB Reports
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• 제29권6호
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• pp.535-539
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• 1996

The activation of phospholipase D (PLD) catalyzes hydrolysis of phosphatidylcholine (PC) to phosphatidic acid (PA) and choline in plants as well as animals. To determine the presence of PLD in oat cells, we prepared inside-out plasma membrane and cytosolic fractions from oat tissues. PLD activities in both cytosol and plasma membrane were detected by ion chromatography method. The activity of PLD in plasma membrane was dependent upon $Ca^{2+}$ concentration and was heat stable. To investigate whether G-protein couples to PLD, the effects of $GTP{\gamma}S$ and $GDP{\beta}S$ on the PLD activity were measured. PLD activity was dramatically increased 300~400% in the presence of 50 ${\mu}M$ $GTP{\gamma}S$ but not in the presence of 50 ${\mu}M$ $GDP{\beta}S$. These results indicate that G-protein may be involved in regulation of PLD activity. To identify whether PLD is regulated by red light receptor, phytochrome, we irradiated red, far-red, or red/far-red/red light on oat protoplasts. PLD activity has increased 5-fold and 3-fold by treatment with red light and red/far-red/red light, respectively. In contrast, irradiation with far-red light had little or no effect on PLD activity. These results suggest that phytochrome regulates PLD activity through activation of G-protein in oat cells.

• 한국식품영양과학회지
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• 제24권4호
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• pp.487-492
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• 1995

The purpose of this study was to investigate the effect of vitamin B2 deficiency on fuel metabolism in streptozotocin-induced diabetic rats. Thirty rats were fed a vitamin B2 deticient diet(-B2) or a control diet (＋B2) for 2 weeks and then subdivided into 3 groups respectively : base group, one day diabetic group and three day diabetic group. Diabetes of the rats were induced by streptozotocin injection into the tail vein. Glucose, glycogen, protein, alanine, triglyceride and free fatty acid were compared in plasma, liver, skeletal muscle of rats. Also, the total urinary nitrogen and glucose excertion were compared. Compared with ＋B2 rats, the increase of plasm glucose in -B2 rats due to the diabetes tended to be smaller. After diabetes were induced, the levels of plasma protein and alanine was significantly decreased and the urinary nitrogen excretion was significantly increased in -B2 rats. The level of plasma free fatty acid was increased continuously in B2 rats while increased at the first day and decreased at the third day diabetes was induced in ＋B2 rats. These results suggest that vitamin B2 deficiency increase protein catabolism due to the decrease of fatty acid oxidation. Thus, vitamin B2 deficiency in diabetes impair the adaptation of animals to the fuel metabolism and aggravate the body protein wasting which is one of the chronic complications of diabetes.

• Journal of Nutrition and Health
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• 제22권1호
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• pp.9-22
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• 1989

The effect of different levels of Zn (0, 30, 300ppm) and protein(7, 20, 40%) in the diet upon lipid metabolism was investigated in Sprague-Dawley male rats weighting 180.54$\pm$29.08g(n=450 fed one of nine diets in a 3$\times$3 factorial design for 5 weeks. The reults obtained were summarized as following. 1) Total lipid contents in serum and liver were tended to be lower in LZn group than CZn and Hzn groups. Those of LP group were higher than CP and HP groups. 2) HDL-cholesterol and total cholesterol contents in serum were significantly affected by dietary Zinc level and were increased as dietary Zinc level increase. 3) Total cholesterol in liver and muscle were tended to be decrease as dietary Zinc level increase. Those in LP group were higher than CP and HP groups. 4) Zinc contents in plasma, liver, muscle and testis were tended to be lower in LZn group than CZn and HZn groups. 5) Protein contents in plasma and liver lower in LZn group than CZn and HZn groups when dietary protein level was 7% and 20%. Those in LP group were lower than those in CP and HP groups. 6) Cu contents in plasma, liver, muscle and testis were tended to be decreased as dietary Zinc level increase.

• Archives of Pharmacal Research
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• 제13권3호
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• pp.233-239
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• 1990

The efect of acute renal failure (ARF) on the pharmacokinetics o sulfobromophthalein (BSP) was investigated in order to elucidate if renal failure modifies the hepatic metabolism of drugs. ARF was induced by intravenous (iv) injection of uranyl nitrate (UN) to rats (5 mg/kg) five days before the experiment. Area under the plasma concentration-time curve (AUC)of BSP after portal vein (pv) injection increased by 2-fold and total body clearance ($CL_1$) decreased one half (p <0.01) in UN-induced ARF (UN-ARF) rate compared to the control rats. But the plasma disappearance of BSP after iv injection did not differ significantly between control and UN-ARF rats. Since BSP is excreted via the liver, $CL_1$ represented the approximate hepatic clearance of BSP. Therefore, the decrease in $CL_1$ represented the approximate hepatic clearance of BSP. Therefore, the decrease in $CL_1$ represents a decrease in hepatic intrinsic clearance ($CL_{int}$) for BSP since plasma free fraction ($f_p$) of BSP was not affected by UN-ARF. The content of hepatic cytoplasmic Y-protein, which catalyzes BSP-glutathione conjugation and limits the trasfer of BSP from blood to bile, increased significantly (p < 0.01), however its binding activity (BA) for BSP was decreased significantly (p <0.01) by UN-ARF. The decrease in $CL_{int}$might have some correlation with the changed characteristics of hepatic Y-protein, specifically its decreased BA for BSP.

• Journal of Periodontal and Implant Science
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• 제23권3호
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• pp.391-398
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• 1993

Gingival crevicular fluid (GCF) is a promising source for markers of destructive periodontal disease activity. This study was undertaken to evaluate the protein composition of GCF in varying stages of the gingival inflammatory response. GCF sampled from 26 people with clinically healthy gingiva and 18 people with periodontitis were examined via sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS/PAGE). The result were as follows. 1. Total amount of GCF protein of diseased group significantly different from that of normal group. But difference in protein concentration was not that significant. 2. In analyzing GCF with SDS/PAGE, it was suggested that albumin is used as indicator plasma protein leakage because of heavily staining bond of albumin in patients with periodontal disease. 3. In diseased group, overall bonds of protein and bands of high molecular weight protein were heavily stained. It was proved useful information on high molecular plasma protein leakage with increasing vascular permeability due to inflammation.

• 한국환경보건학회지
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• 제3권1호
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• pp.45-47
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• 1976

A survey was carried out in order to figure out of phenomenon by school feeding from June 1973 to May 1974. Hematological values and plasma protein of 94 boys and 91 girls (total 185 students)were studied. As the results of this survey, the following conclusions were obtained. 1. Hemoglobin, hematocrit, mean corpuscular hemoglobin concentration of boys and girls were increased after school lunch. 2. Plasma protein of boys and girls were clearly increased after school lunch.

• Archives of Pharmacal Research
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• 제15권2호
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• pp.184-186
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• 1992

Malonic acid amides were synthesized using different amino acids and their esters. THe synthesized compounds were evaluated for their sedative activity on rats. Potentiating effect of all the compounds on pentobarbitone induced sleep on rats was observed. Plasma protein binding studies were also carried out and it was observed that the synthesized compounds have low plasma protein binding as compared to barbiturates.

• Archives of Pharmacal Research
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• 제25권6호
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• pp.759-769
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• 2002

Mutated forms of ras are found in many human tumors and the rate of incidence is significantly higher in colon and pancreatic cancers. The protein product from the ras oncogene is a small G-protein, $p21^{ras}{\;}(Ras)$ that is known to playa key role in the signal transduction cascade and cell differentiation and proliferation. Mutated Ras is unable to regulate itself and remains constantly activated, leading to uncontrolled cell growth. The function of Ras in signal transduction requires its location near the growth factor receptor at the cell membrane. However, Ras does not have a transmembrane domain. Ras requires farnesylation to increase its hydrophobicity and subsequent plasma membrane association for its transforming activity. This key post-translational modification is catalyzed by the enzyme Ras farnesyltransferase (FTase), which transfers a farnesyl group from farnesylpyrophosphate to the C-terminal cysteine of the Ras protein. The requirement has focused attention on FTase as a target for therapeutic intervention. Selective inhibition of FTase will prevent Ras protein from association with the plasma membrane, leading to a disruption of oncogenic Ras function.