• Title/Summary/Keyword: eletrophoretic patterns

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Changes in Chromatographic Fractionation and Composition of the Proteins of Malting Barley Grain during Germination (발아기간별 맥주맥 단백질의 분획 및 조성변화)

  • Seo, Ho-Soo;Cho, Sung-Hwan
    • Korean Journal of Food Science and Technology
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    • v.24 no.1
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    • pp.1-6
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    • 1992
  • Changes in protein distributiun, eletrophoretic patterns and amino acid composition were investigated during germination of malting barley. Fractionation of the protein complex in ungerminated malting barley resulted in a higher hordein fraction but less glutelin fraction of the protein complex in ungerminated malting barley resulted in a higher hordein fraction but less glutelin fraction as compared to germinated malting barley. As germination proceeded, NPN, globulin and glutelin fractions continued to increase, accmpanied by decreases in albumin and hordein fractions. The electrophoretic pattern of malting barley proteins showed three bands (molecular weight range of $15,000{\sim}41,000$ daltons) in albumin fraction, five bands ($19,000{\sim}61,000$ daltons) in globulin fraction, five bands ($18,000{\sim}56,000$ daltons) in hordein fraction and tour bands ($20,000{\sim}47,000$ daltons) in glutelin fraction, exhibiting quantitative changes in each fraction during germination. Amino acid analysis showed that glutamic acid, histidine, aspartic acid, serine, glycine, valine, alanine and leucine were major amino acids of proteins in malting barley grains. Glutamic acid increased slightly, but other amino acids showed no definite trend as germination proceeded.

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Sugar Content and Protein Fractionation in Human Pleural Fluid (늑막액의 당 및 단백분획상)

  • Kim, W.J.;Ahn, Y.S.;Kim, H.Y.;Lee, W.Y.
    • The Korean Journal of Pharmacology
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    • v.15 no.1_2 s.25
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    • pp.1-5
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    • 1979
  • Previous studies concerning the usefulness of pleural fluid glucose levels in differentiating causes of pleural effusions have been conflicting. Gelenger and Wiggers (1949), Calnan et al(1951) and Barber et al(1957) concluded that the lower the level of pleural fluid glucose, the more likely was tuberculosis, and that tuberculosis was unlikely if the pleural fluid glucose level was more than 80 mg/100 ml. Light and Ball(1973), however, reported that in the great majority of tuberculous pleural fluids the glucose concentration was high rather than low, concluded that the pleural fluid glucose levels were not useful in the differential diagnosis of pleural effusion. In this study, pleural fluid glucose was determined in 46 pleural effusions from various causes to evaluate the usefulness in the differential diagnosis of pleural effusion. In addition, the protein concentration and the electrophoretic patterns of protein and amylases in pleural fluid was compared with that of serum. And the results were as follows. 1. The mean glucose concentration of pleural fluid was 80.8 mg/100 ml in 22 tuberculous origin, 92.5 mg/100 ml in 12 cancer patient and 70.4 mg/100 ml in 10 undiagnosed cases. In 2 cases of paragonimiasis the pleural fliud glucose levels were low (mean, 32.0 mg/100 ml). The percentage of pleural fluid protein to serum is about 75% in all disease groups and the protein level of tuberculous pleural fluid was significantly correlated with that of serum. 2. The disc eletrophoretic patterns of pleural fluid were almost similar with that of serum in all disease groups but the prealbumin fraction was not observed in pleural fluid. 3. With the isoelectric focusing, 4 to 7 isoamylase was observed in serum and the isoelectric point was ranged from pH 5.8 to 7.8 and isoelectic point of main fracticn is pH 7.2. The isoelectic focusing patterns of amylase of pleural fluid were identical to that of serum in all disease group. With the above results it is concluded that the pleural fluid is exudate of serum and that the glucose levels of pleural fluid are not useful in the differential diagnosis of pieural effusions.

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Electrophoretic analysis of the major protein of erythrocyte membrane in man, bovine, horse, and dog: their relation to erythrocyte sedimentation rate (사람, 소, 말, 개의 적혈구막 단백의 전기 영동법에 의한 분석 - 적혈구 침강 속도와의 관계 -)

  • Bahk, Yeong-woo
    • Korean Journal of Veterinary Research
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    • v.41 no.1
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    • pp.21-28
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    • 2001
  • The protein of the bovine, horse and dog erythrocyte membrane were analyzed by polyacrylamide gel eletrophoresis in sodium dodecyl sulfate and their relation to the sedimentation rate of animal erythrocytes were investigated by treating the erythrocytes with proteinases such as trypsin and chymotrypsin. Protein content in erythrocyte membrane was in human, in Jindo dog, in cattle and in horse, showing similar in among. The erythrocyte sedimentation rates bovine erythrocytes from Hostein and Korean native cattle were very slow compared with the human one(1/7 as slow as the human one) as reported previously. Although the general protein profiles of the bovine erythrocyte membranes were almost similar to that of human, bovine erythrocyte membranes showed one additional protein band, called band Q in this study, which migrated electrophoretically to the mid-position between band 2 and band 3 in human erythrocyte membranes. The erythrocyte sedimentation of race horse were very fast compared with the human one are reported previously. Although the general protein profiles of the race horse erythrocyte membranes were almost similar to that of human, band 3 content was showing higher in race horse(34.7%) than in human(25.3%). The general protein profile of the Jindo dog erythrocyte membrane was almost similar to the human patterns, Jindo dog erythrocyte membranes showed one absent protein band. It was band 7. The glycoprotein profiles of the bovine erythrocyte membranes revealed by periodic acid-Schiff(PAS) stain showed a marked difference from that of human. The PAS-1(glycophorin) and PAS-2(sialoglycoprotein) present in human erythrocyte membrane were almost absent from the bovine erythrocyte membranes showed a strong PAS-positive band near the origin of the electraphorograms, which is named as PAS-B in this study. The PAS-1 and PAS-2 present in human erythrocyte membrane were almost absent from race horse erythrocyte membranes, but PAS-2 was more in only race horse from that of human. The PAS-1 and PAS-2 were absolutely absent from the Jindo dog erythrocyte membrane. These results suggest the slow sedimentation rate of bovine erythrocytes is due in part to the presence of band Q protein fraction and PAS-B glycoprotein in the bovine erythrocytes, and that the fast sedimentation rate of race horse erythrocyte is due in part to the presence of more band 3 protein fraction and PAS-E glycoproteins in the race horse erythrocytes.

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