• Korean Journal of Veterinary Service
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• v.15 no.2
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• pp.128-133
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• 1992

To obtain the basic data for blood chemistry, the effects of the time elapse of serum separation on bovine blood chemical values were investigated. The results obtained are summerized as follows : 1. The constant fluctuation tendency and significance was not detected in GOT, GPT, BUN, Creatinine, ALP, CPX, Cholesterol, Ca, Mg and Pi. 2. Glucose showed the decrease tendency according to the time elapse of serum separation. As the values at 12 and 24 hours showed significant lower values than those at 1 and 2 hours (p＜0.01) it was thougth that separation time of serum should be focussed for the glucose determination.

• Korean Journal of Veterinary Research
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• v.29 no.2
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• pp.33-39
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• 1989

Pure separation of various leukocytes is required for the assessment of their roles in immunological and phisiological function. In this study, pure separation of monocytes from canine peripheral blood was attempted. At first, mononuclear cells (PBMC) were separated by ficoll-hypaque gradient method and then monocytes were recovered from PBMC suspensions in sucrose gradient Sol. (PBMC-Sucrose), autologous plasma (PBMC-Plasma) and autologous serum (PBMC-Serum) incubated at $37^{\circ}C$ for 2 hours. 1. In the separation of PBMC by ficoll-hypaque gradient method in canine blood, higher relative centrifugal force (RCF) was required, as high as more than 1,300xg RCF for 40 minutes, for clear formation of PBMC layer than that in human blood as usually used 400xg RCF for 40 minutes. 2. In monocytes-separation from three PBMC suspensions following PBMC separation, recovery-, purity- and viability-rate of monocytes showed better results in PBMC-Plasma and PBMC-Serum than in PBMC-Sucrose suspension, particulary showing better results from PBMC suspensions performed by centrifugation at 1,500xg RCF for 40 minutes.

• Membrane and Water Treatment
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• v.2 no.2
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• pp.91-103
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• 2011

The flux behavior in the separation of equimolar bovine serum albumin (BSA) and bovine hemoglobin (HB) in aqueous solutions by cross-flow ultrafiltration (UF) was investigated, in which polyacylonitrile membrane with a molecular weight cut-off (MWCO) of 100 kDa was used. BSA and HB have comparable molar mass (67,000 vs. 68,000) but different isoelectric points (4.7 vs. 7.1). The effects of process variables including solution pH (6.5, 7.1, and 7.5), total protein concentration (1.48 and 7.40 ${\mu}M$), transmembrane pressure (69, 207, and 345 kPa), and solution ionic strength (with or without 0.01 M NaCl) on the separation were examined. It was shown that the ionic strength had a negligible effect on separation performance under the conditions studied. Although BSA and HB are not rigid bodies, the flux decline in the present cross-flow UF did not result from the mechanism of cake filtration with compression. In this regard, the specific cake resistance when pseudo steady-state was reached was evaluated and discussed.

• Korean Journal of Food Science and Technology
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• v.19 no.3
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• pp.225-230
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• 1987

The foam separation of bovine serum proteins was investigated and the protein fractionation by foam separation was analyzed by PAG electrophoresis. The protein concentration for the surface excess formation of bovine serum was in the range of $20-800\;{\mu}g/ml$. At pH 5, the foamate volume was maximum, but the enrichment ratio minimum. As the temperature was elevated, the foamate volume decreased and the enrichment ratio increase. As the gas flow rate increased from 25 to 100 ml/min, the foamate volume decreased and the enrichment ratio increased. The enrichment ration became maximum when the added ionic strength of serum solution was in the range of 1-3 by the addition of different types of salts, and this was related to the reduction of surface tension of the solution. In general, BSA, ${\alpha}_1$, and ${\alpha}_2-globulins$, which have relatively small molecular weight and high hydrophobicity, moved easily to the foam, and the separation of protein fractions in the serum varied with the changes in pH, temperature, gas flow rate and ionic strength of the solution.

• Bulletin of the Korean Chemical Society
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• v.34 no.12
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• pp.3817-3824
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• 2013

Various separation modes in HPLC, such as anion exchange (AE), reversed-phase (RP), and affinity (AF) chromatography were examined for the separation of selenium species in human blood serum and urine. While RP- and AE-HPLC were mainly used for the separation of small molecular selenium species, double column AF-HPLC achieved the separation of selenoproteins in blood serum efficiently. Further, the effluent of AF-HPLC was enzymatically hydrolyzed and then analyzed with RP HPLC for selenoamino acid study. The versatility of the hybrid technique makes the in-depth study of selenium species possible. For quantification, post column isotope dilution (ID) with $^{78}Se$ spike was performed. ORC ICP/MS (octapole reaction cell inductively coupled plasma/mass spectrometry) was used with 4 mL $min^{-1}$ Hydrogen as reaction gas. In urine sample, inorganic selenium and SeCys were identified. In blood serum, selenoproteins GPx, SelP and SeAlb were detected and quantified. The concentration for GPx, SelP and SeAlb was $22.8{\pm}3.4\;ng\;g^{-1}$, $45.2{\pm}1.7\;ng\;g^{-1}$, and $16.1{\pm}2.2\;ng\;g^{-1}$, respectively when $^{80}Se/^{78}Se$ was used. The sum of these selenoproteins ($84.1{\pm}4.4\;ng\;g^{-1}$) agrees well with the total selenium concentration measured with the ID method of $87.0{\pm}3.0\;ng\;g^{-1}$. Enzymatic hydrolysis of each selenium proteins revealed that SeCys is the major amino acid for all three proteins and SeMet is contained in SeAlb only.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.17-22
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• 2000

The separation of tryptophan enantiomers was carried out with medium-pressure liquid chromatography using BSA (bovine serum albumin)-bonded silica as a chiral stationary phase. The influence of various experimental factors such as pH and ionic strength of mobile phase, separation temperature, and the presence of organic additives on the resolution was studied. In order to expand this system to preparative scale, the loadability of sample and the stability of stationary phase for repeated use were also examined. The separation of tryptophan enantiomers was successful with this system. The data indicated that a higher separation factor (a) was obtained at a higher pH and lower temperature and ionic strength in mobile phase. Addition of organic additives (acetonitrile and 2-propanol) in mobile phase contributed to reduce the retention time of L-tryptophan. About $30\%$ of the separation factor was reduced after 80 days of repeated use.

• Applied Biological Chemistry
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• v.40 no.1
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• pp.48-52
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• 1997

Modified starches were used as additives to make tomato ketchup, and their effects on the rheological properties, serum separation and sensory characteristics of the tomato ketchup were examined. The magnitudes of the yield stress and the consistency index of the tomato ketchup with the additives, regarded as a Herschel-Bulkley fluid, were found to be in the order of ADA(acetylated distarch adipate)>SA(starch acetate) >HDP(hydroxypropyl distarch phosphate)>RCS(raw corn starch)>NS(no starch). The flow behavior indices of SA added ketchup and HDP added one were nearly constant regardless of the additive concentrations, whereas those of ADA and RCS increased with the additive concentration. In the serum separation test centrifugation, the ADA added ketchup showed the highest stability against separation, being fol-lowed by SA>HDP>RCS>NS. In the sensory evaluation, the magnitudes of the acceptance of the ketchup with the additives were as ADA(2%)>SA(2%)>RCS(2%)>NS>HDP(2%).

• Macromolecular Research
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• v.13 no.1
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• pp.39-44
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• 2005

Ion-exchange polymeric stationary phases presenting amino acid and amino groups were prepared by the surface grafting of glycidyl methacrylate onto a silica gel surface and subsequent amination. Three kinds of amino acids-L-arginine (Arg), D-lysine (Lys), and D-histine (His)-were used in this study. An ion-exchange polymeric stationary phase presenting ethylene diamine (EDA) was also prepared by surface graft polymerization. Separation of the model proteins bovine serum albumin (BSA), chick egg albumin (CEA), and hemoglobin (Hb) was performed using the amino acid- and amine-derived columns. In separating the CEA/BSA mixture, the resolution time of BSA was longer than that of CEA when using the EDA column, whereas the resolution time of BSA was shorter than that of CEA when using the Arg, Lys, and His columns. In the separation of the Hb/BSA mixture, the resolution time of BSA was longer than that of Hb in the EDA column, whereas the resolution time of BSA was shorter than that of Hb in the amino acid columns (D-Lys, L-Arg, and D-His).

• KSBB Journal
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• v.9 no.2
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• pp.98-103
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• 1994

A bed configuration wherein sheets of modified fibrous polyethylene are potted within a Millipore Filter Cartridge matrix has been developed. Polyethylene fibers form sturdy beds but the native hydrophobicity and inertness of polyethylene have precluded their use in protein chromatography The polyethylene fibers used in this system were modified by plasma oxidation and further derivatization. The resulting fibers are hydrophilic, bind protein reversibly and serve as an anion-exchange stationary phase. Separation of Bovine Serum Albumin on this bed, as well as results of basic studies on capacity and reversibility of binding within a fibrous bed and experimental data handling system are shown.

• Korean Journal of Veterinary Research
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• v.11 no.2
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• pp.145-148
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• 1971

Serum Samples from adult of Korean cattles including 40 females and 20 males were analyzed by sodium salt precipitation and colorimetric method in the purpose of the determination of total serum protein, albumin, globulin, ${\alpha}$-globulin, ${\beta}$-globulin and ${\gamma}$-globulin. The results obtained arc summarized as follows: 1. Mean value of total serum protein showed a slight variation from 7.6%, and its regional and sex differences were not found to be significant. 2. Contents of albumin in serum showed lower level than that of globulin as low level of A/G ratio 0.4 in proportion. 3. Contents of Serum ${\alpha}$-globulin showed 1.4w/v% and $1.51{\pm}0.46$w/v% in each group of female, and $1.31{\pm}0.26$w/v%, in the group of male. 4. Contents of serum ${\beta}$-globulin showed 1.74w/v%, 1.95w/v%, in each group of female, and 1.82w/v% in the group of male. 5. Contents of serum ${\gamma}$-globulin showed 2.32w/v%, 2.30w/v% in each group of female, and 2.30w/v%, in the group of male.