• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.2
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• pp.195-198
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• 1989

The water binding capacity (WBC) of hoe plasma protein was investigated. The centrifugal condition for optimal separation of plasma from hog blood was fixed at 1400 g-force. The WBC of 5%-plasma-protein-solution eel increased rapidly between pH 6 and 7 but gradually after pH 7 at $85^{\circ}C$ for 30 min. The higher heating temperature demonstrated the higher WBC of 5%-plasma-protein-solution gel at pH 7 within short period of time. The WBC of 5%-plasma-protein-solution gel increased rapidly at the beginning of heating. The WBC per gram of plasma protein at pH 7 and $85^{\circ}C$ for 30 min decreased as protein concentration of the plasma solution increased.

• Applied Biological Chemistry
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• v.39 no.2
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• pp.123-126
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• 1996

Simple and rapid method of purification of plasma proteins from bloods of slaughtered animals was developed and the proteins were applied to plywood products as a blood 히ue to utilize waste materials. Plasma protein was obtained by adding 2% trichloroacetic acid (TCA) or 0.6 N HCI as optimal concentration to the supernatant, after centrifugation of bloods. Molecular properties of beef and pig plasma proteins were examined on SDS-PAGE. Application of blood glue to plywood was quite satisfactory compared to the synthetic amino resin by tensile-shear test for the strength of adhesive bonding.

• Korean Journal of Food Science and Technology
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• v.25 no.3
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• pp.295-298
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• 1993

This study was carried out to investigate the effects of heating temperature, heating time and protein concentration on the gel properties and heat stability of a mixed system of pork plasma and myofibrillar to increase the utility of porcine blood as protein resources of the food industry, especially meat processing industry. The solubility of plasma protein and mixture (plasma + myofibrillar protein) decreased significantly at $70^{\circ}C\;to\;90^{\circ}C$ when heating temperature rised, whereas myofibrillar protein decreased slightly at $40^{\circ}C\;to\;60^{\circ}C$, and the gel strength and the turbidity of those increased significantly at these heating temperatures. The solubility of plasma protein and mixture decreased when the heating time increased at $75^{\circ}C$, whereas the gel strength and turbidity increased, and the solubility, the gel strength and the turbidity of myofibrillar protein showed no changes.

• Korean Journal of Food Science and Technology
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• v.30 no.4
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• pp.988-991
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• 1998

Plasma proteins were obtained from bloods of slaughtered bovine and porcine and analyzed by Fast Protein Liquid Chromatography (FPLC). Serum albumin content decreased in the following order: Porcine Plasma Protein (PPP)> Bovine Plasma Protein (BPP)> Whey Protein Concentrate (WPC). Protein contents of BPP, PPP, and WPC determined by Kjeldahl method were 85.79%, 82.30%, and 84.38%, respectively. Compared to WPC, plasma proteins had higher emulsifying activity index (EAI) below 2% protein concentration and slightly lower EAI above 4% protein concentration. Plasma proteins had higher EAI in the acidic pH range and more dependence on NaCl than WPC. Also, EAI of plasma proteins with NaCl was higher in the acidic range than that of WPC. These results indicated that plasma protein can be utilized as a raw material for emulsifier.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.428-432
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• 1991

This study was carried out to investigate the effect of NaCl, pH and phosphate on the functional properties of a mixed system of plasma protein and myofibrillar proteins. The solubility of plasma protein, myofibrillar protein and the mixture (plasma+myofibrillar protein) increased according to the increase of NaCl concentration ($0{\sim}4%$) and pH $pH4{\sim}8$). The solubility, emulsifying activity and capacity of the mixture were lower than those of plasma protein, whereas higher than those of myofibrillar protein. The gel strength of the mixture and myofibrillar protein showed a significant increase when NaCl concentration was increased from 2 to 3%. The gel strength of myofibrillar protein increased about four times when 0.3% polyphosphate added to the sample containing 2% NaCl, whereas the moisture loss of the mixture and myofibrillar protein decreased significantly. The gel strength of plasma protein, myofibrillar protein and the mixture increased slightly at $3{\sim}5%$ protein concentration, whereas the gel strength of those increased significantly as the protein concentration increased from 5 to 9%.

• Applied Biological Chemistry
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• v.40 no.1
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• pp.39-42
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• 1997

Angiotensin converting enzyme (ACE) inhibitors were isolated and purified from pig blood plasma. Pig blood plasma was obtained after removing blood cells by centrfugation, followed by the addition of anticoagulant to whole pig blood. To precipitate plasma proteins, pig blood plasma was treated with 4% trichloroacetic acid (TCA) as a final concentration. ACE inhibitors were isolated from plasma protein hydrolysates and TCA supernatant, using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. ACE inhibitors isolated from plasma hydrolysates and TCA supernatant had $IC_{50}$ values of $23\;{\mu}M$ and $2\;{\mu}M$, pentapeptide, respectively.

• KSBB Journal
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• v.18 no.2
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• pp.100-106
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• 2003

An on-line frontal analysis HPLC system was developed to determine the unbound concentration of (S)-perillyl alcohol, an potential anti-cancer agent, in human serum albumin (HSA) solution, The analysis was performed on a Develosil 100 Diol 5 (10 cm x 4.6 mm I.D.) high-performance frontal analysis (HPFA) column. Sodium phosphate solution was used as the mobile phase (pH 7.4, ionic strength 0.17) at a flow rate of 1 $m\ell$/min. UV wavelength was set at 205 nm. A injection volume of 600${mu}ell$ was chosen to ensure the compound eluted formed a zonal peak with a plateau. By Scatchard analysis, it was found that the binding constant(K) and binding number(n) of (S)-perillyl alcohol to molecular HSA were 2.05 x $10^6$ [$M{-1}$], 0.00428, respectively.

• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.658-664
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• 1999

Broiler and porcine blood plasma were desugarized by GOD (glucose oxidase 10 units/g) or baker's yeast (0.3% w/w) and dried. The color, biuret protein content, solubility, foaming capacity and pH of desugarized blood plasma powder during storage at room temperature were investigated. Desugarized plasma powder was lighter and less red and yellow than the control group (P<0.05). Biuret protein content and solubility of deglucosed plasma powder were higher than the control. Biuret protein content and solubility of all samples decreased during storage (P<0.05). Generally, deglucosed samples showed better foaming capacity than the controls (P<0.05). The pH of deglucosed broiler samples by yeast and porcine samples were decreased just after initial increasing, while the pH of other broiler powder was continuously decreased during storage. Deglucosed porcine powder always showed higher pH values than the control (P<0.05). Overall, desugatization of broiler or porcine blood plasma before drying improved color, biuet protein content, solubility and foaming capacity.

• Journal of Nutrition and Health
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• v.19 no.5
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• pp.296-303
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• 1986

Rat lipoprotein-deficient plasma possessed a lipid tramsfer inhibitory activity when it was added to purified human plasma lipid transfer protien, while it lacked a lipid transfer activity. Incubation of whole rat plasma with partially purified human lipid transfer protein resulted in big changes in lipid distribution of rat plasma lipoproteins. There w was a 4-fold increase in cholesteryl ester(CE) and 4 47 % reduction in triglyceride(TG) in very low density lipoproteins after 2싹lour incubation. In high density lipoprotein $2(HDL_2)$ there was a 9­fold increase in TG and 33 % reduction in CEo HDL3 had 82 % reduction in CE. The result indi­c cates that the absence of the lipid transfer activity in rat plasma can be ascribed not to the inability of rat lipoproteins to serve as substrates but to the lack of 야Ie lipid transfer protein in rat plasma. Th­e erefore, species differences in lipid transfer betwe­e en lipoproteins should be taken into consideration to interpret results of studies on lipoprotein m.eta­b bolism using rats.

• Korean Journal of Food Science and Technology
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• v.29 no.5
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• pp.1067-1070
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• 1997

Imunoglobulins from bovine plasma proteins were isolated by IMAC which $Cu^{2+}$ was chelated on a chelating sepharose fast flow gel. Most plasma proteins were eluted by 1st (0.01 M $Na_2HPO_4$, 0.5 M NaCl, pH 4.0) and 2nd elution buffers (0.01 M imidazol). According to the reverse phase HPLC analysis, it was found that proteins which were eluted by 1st elution buffer were mainly composed of serum albumin, while most IgG and transferrin were eluted by 2nd elution buffer. When protein fractions obtained by 2nd elution buffer was applied to ultra filtration system (molecular weight cut off: 100 kD), IgG was further purified. These results indicate that IMAC is an excellent tool for isolating imunoglobulins from plasma proteins.