• Journal of Pharmaceutical Investigation
• /
• v.6 no.2
• /
• pp.88-94
• /
• 1976

This paper attempted to investigate the effect of pretreatment with carbon tetrachloride on absorption, excretion, protein binding, and biological half-life of sulfisoxazol from rats and rabbits. Absorption of sulfisoxazol was found to decrease in severe damage rats, compared with that of normal rats, but in mild rats, absorption of sulfisoxazol was similar to that of nomal rats. Absorption of sulfisoxazol was decreased significantly in severe damage rabbit pretreated with carbon tetrachloride but in mild damage rabbit, absorption of sulfisoxazol was not influenced significantly. Pretreatment with carbon tetrachloride gave the effect on clearance of sulfisoxazol in part but protein binding percent of sulfisoxazol was not influenced by concentration of carbon tetrachloride.

• Journal of Photoscience
• /
• v.9 no.2
• /
• pp.126-129
• /
• 2002

The chromophore/protein interactions in the photocycle intermediates of photoactive yel- low protein (PYP) were probed by site-directed mutagenesis. The absorption spectra of L- intermediates produced from E46Q, T50V, and R52Q mutants were calculated using the absorption spectra of dark states and difference absorption spectra between L-intermediates and dark states, and compared with that of PYP$\_$L/. The absorption spectrum of R52Q$\_$L/ agreed with that of PYP$\_$L/, but those of E46Q$\_$L/ and T50V$\_$L/ were red-shifted. The effect of these mutations on the absorption spectrum for L-intermediate was comparable to that for the dark state, suggesting that the interaction around the phe-nolic oxygen of the chromophore is conserved in PYP$\_$L/ unlike the crystal structure. On the other hand, we have reported that the absorption spectra of Y 42F$\_$M/, T50V $\_$M/, and R52Q$\_$M/ agreed with that of PYP$\_$M/, but that of E46Q$\_$M/ was red-shifted, suggesting that the hydrogen bond of the chromophore with Glu46 is conserved but that with Tyr42 is broken in PYP$\_$M/. These results suggest that the chromophore inter-acts with Glu46 throughout the photocycle, but never directly interacts with Arg52. This model con- flicts with some of the structural model of PYP intermediates proposed based on the high-resolution X -ray crystallography.

• The Korean Journal of Food And Nutrition
• /
• v.9 no.3
• /
• pp.319-324
• /
• 1996

The functional properties of protein recovered from red crab (Chitinonecetes opiiie) processing in water (RCP) were examined and compared with those of soybean protein isolate at pH 2~10 in water and NaCl solu5ion. The solubilities of RCP and SPI were miniumu at pH 4, the isoelectric point and increased significantly at lower or higher than pH 4. Solubilities in NaCl solution for both proteins decreased with incr NaCl concentration increase at all pH ranges. Emulsion capacity for both proteins was also minimum at pH 4 and increased as protein concentration increased from 2 to 6%. Emulsion capacity of RCP was higher than these of SPI at pH 6∼10 and all protein concentrations. Emulsion stability showed a similar trend to that of emulsion capacity. RCP had higher oft absorption capacity and lower water absorption capacity than SPI.

• Journal of Pharmaceutical Investigation
• /
• v.25 no.4
• /
• pp.291-298
• /
• 1995

The purpose of this study is to verify the interaction between food and ampicillin which is one of the aminopenicillins known to be absorbed by a specified dipeptide transporter in the small intestine. The absorption of ampicillin was measured in the presence of the high carbohydrate food, high fat food, and high protein food, and compared with that in the presence of the control normal food. In situ single-pass perfusion method was chosen in these experiments using two jejunal segments in the rat. Reduction in the absorption of ampicillin was not shown, when both high carbohydrate food and high fat food were co-perfused with ampicillin. When the high protein food was co-perfused with ampicillin, the difference of $C_{out}/C_{in}$ of ampicillin ratio was $0.084\;{\pm}\;0.082$, showing a trend of reduced absorption without a significance. Further, glyclysarcosine (Gly-Sar) which is a stable dipeptide in the small intestine was used in order to see the direct competitive inhibition with ampicillin on the dipeptide transporter. The difference of $C_{out}/C_{in}$ ratio was $0.078\;{\pm}\;0.020$ in the presence of 10 mM Cly-Sar, showing a significant inhibition of ampicillin absorption (p < 0.02). It suggests that dietary di- and tripeptides, the digestive products of protein food, might have influence on the absorption of ampicillin, and that ampicillin could be given at the lasting state for better absorption.

• Journal of Crop Science and Biotechnology
• /
• v.10 no.3
• /
• pp.133-140
• /
• 2007

Protein characteristics of Korean wheat were evaluated to determine the effects of protein content and quality on processing and textural properties of white salted noodles compared to US wheat flours with various wheat classes and commercial flours for making noodles. Protein quality parameters, which were independent of protein content and included SDS sedimentation volume with constant protein weight, mixograph mixing time and proportion of 50% 1-propanol insoluble protein, of Korean wheat flours with 2.2+12 subunits in high molecular weight glutenin subunit compositions were comparable to those of commercial flours for making noodles. Parameters related to noodle making, including optimum water absorption, thickness and color of noodle dough sheet, correlated with protein content and related parameters, including SDS sedimentation volume with constant flour weight, mixograph water absorption and gluten yield. No significant relationship was found in protein parameters independent of protein content. Hardness of cooked noodles from Korean wheats was lower than that of US wheat flours compared to similar protein content of commercial noodle flours. Adhesiveness, springiness and cohesiveness of cooked noodles from Korean wheats were similar to US wheat flours. Hardness of cooked noodles correlated with protein content and related parameters.

• Asian-Australasian Journal of Animal Sciences
• /
• v.25 no.10
• /
• pp.1457-1465
• /
• 2012

Intestinal phosphate (Pi) absorption across the apical membrane of small intestinal epithelial cells is mainly mediated by the type IIb Na-coupled phosphate co-transporter (NaPi-IIb), but its expression and regulation in the chicken remain unclear. In the present study, we investigated the mRNA and protein levels of NaPi-IIb in three regions of chicken small intestine, and related their expression levels to the rate of net phosphate absorption. Our results showed that maximal phosphate absorption occurs in the jejunum, however the highest expression levels of NaPi-IIb mRNA and protein occurs in the duodenum. In response to a low-Pi diet (TP 0.2%), there is an adaptive response restricted to the duodenum, with increased brush border membrane (BBM) Na-Pi transport activity and NaPi-IIb protein and mRNA abundance. However, when switched from a low-(TP 0.2%) to a normal diet (TP 0.6%) for 4 h, there is an increase in BBM NaPi-IIb protein abundance in the jejunum, but no changes in BBM NaPi-IIb mRNA. Therefore, our study indicates that Na-Pi transport activity and NaPi-IIb protein expression are differentially regulated in the duodenum vs the jejunum in the chicken.

• Journal of Pharmaceutical Investigation
• /
• v.6 no.1
• /
• pp.18-25
• /
• 1976

The purpose of this investigation was to determine the effect of ethanol on the absorption, excretion and protein binding of sulfadimethoxine from the small intestine of the rat and rabbit. The results are as follows: 1. The rat small intestinal absorption of sulfadimethoxine was increased by 0.5% and 2% ethanol. 2. Blood level of sulfadimethoxine after oral administration was significantly elevated (p<0.01) by 0.5g/kg and 1g/kg ethanol respectively, but was significantly inhibited by 3g/kg ethanol from that of the control. 3. Ethanol gave the effect on the clearance of sulfadimethoxine, which was increased by ethanol from that of control. 4. In the protein binding rate, it was found that ethanol decreased protein binding of sulfadimethoxine except 0.1% and 0.5% ethanol.

• Journal of Nutrition and Health
• /
• v.30 no.3
• /
• pp.266-276
• /
• 1997

To investigate the effects of dietary protein and calcium levels on calcium and bone metabolism Sprague-Dawley male growing rats weighting approximately 91.4g were divided into four groups and fed one of the following four experimental diets-15% protein 0.2% calcium ; 15% protein 0.5% calcium ; 30% protein 0.2% calcium ; 30% protein 0.5% calcium-for five weeks. Calcium intake and excretion, apparent calcium absorption were measured and bone densities and mineral contents of femur and scapula were analyzed. Calcium excretion through feces and urine was significantly greater in animals receiving diets of higher calcium. Fecal calcium but not urinary calcium excretion was greater when the protein level was increased from 15% to 30%. Apparent calcium absorption rate was significantly higher with lower calcium intakes. Serum alkaline phosphatase activity was significantly higher in 0.2% calcium group than in 0.5% calcium group, while urinary hydroxyproline excretion was essentially same among all experimental groups. Weights and mineral contents or protein. Bone weights were greater, but calcium and ash contents of femur and scapula were lower in animals on the diet containing low calcium and high protein, which suggests that bone metabolism may be affected by the interaction between calcium and protein intake. These results indicate that during growth high protein intake might be beneficial to bone health if the diet is sufficient in calcium, however, if the diet fails to provide an optimum amount of calcium, such practice might be detrimental.

• Korean Journal of Plant Resources
• /
• v.11 no.3
• /
• pp.272-278
• /
• 1998

This study was carried out to investigate the functional properties such as nitrogen solubility, emulsifying property , foaming capapcity , water and oil absorption of Camellia (Camellia japonica .) seed protein isolate in condition of distilled water and 0.5M NaCl solution at pH 2.0∼10.0. Nitrogen solubility of Camellia protein isolate in distilled water showed the minimum value at pH 4.0 and increased at pH lower or higher than the isoelectric point(pH 4.0). It was 90.0 %at pH 10.0 Nitrogen solubility of 0.5M NaCl solution showed a similar pattern with that of distrille dwater but was higher than that of distilled water except pH 2.0 and pH 10.0. Emulsifying activity of Camellia seed protein islate showed the minimum value at pH 4.0, but was higher at ether value of pH. Emulsifying stability of protein isolate was stable by heat treatment for 30min, at 80℃ and increased in 0.5M NaCl solution more than that of distille dwater. Foaming capacity of Camellia seed protein isolate in distill3ed water showed the minimum value near the isoelectric point, While it changed little at other values of pH. Foaming stability slowly decreased as, but didn't make a significant difference as time was delayed . Oil absorption was 1.4ml per a sample of 1g and water absorption was 0.9ml per a sample of 1g. The former was higher than the latter . The content of total amino acid of Camellia protein isolate was 43.67% and the major total amino acid of Camellia protein isolate was 43.67% and the major total amino acid was in the order of glutamic acid , arginine, aspartic acid, and leucine.

• Journal of the East Asian Society of Dietary Life
• /
• v.10 no.5
• /
• pp.394-403
• /
• 2000

The functional properties of sesame protein concentrate(SPC) using different size of ultrafiltration(UF) membranes were examined and compared with those of conventional acid-precipitated sesame protein concentrate. The protein contents of SPC by UF with molecular size of 10K, 30K and look dalton membranes were 84.2%, 82.7%, and 76.4%, respectively, and that of acid-precipitated SPC was 88.7%. The nitrogen solubility of SPC by UF was higher than that of conventional SPC at various pH levels. Especially, it showed three-fold increase at near isoelectric point. However, water absorption capacity and fat absorption capacity of SPC by UF were decreased. For emulsion and foam properties, there were no significant differences between SPC by acid precipitation and SPC by UF method. At various pH levels, SPC by membrane with pore size of 30K dalton showed the highest emulsion properties. The SPC by UF had slightly higher viscosity than defatted sesame flour and SPC by acid precipitation.