• 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.

• Korean journal of applied entomology
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• v.32 no.4
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• pp.420-425
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• 1993

The programme of silkrnoth chorion protem synthetIc changes is autonomous i. e.,it is imple I mented WIth normal kinetics by follicles cultured in isolation in a defined tIssue culture medium. On the basis of protem synthetic profiles, 8 stages of chorwgenesis are defined. Detail a analysis of the proteins of chorion of Bombyx mandarina, reveals more than 17 components by eletrophoretic mobility and synthetic kinetics. We have defined three abbreviated synthetlc s stages, based on the pattern of protein synthesized at early, middle, and late synthetic stages

• 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.

• Korean Journal of Food Science and Technology
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• v.15 no.2
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• pp.128-132
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• 1983

The apple seed contained 25.96% of crude fat and 37.62% of crude protein. The lipid fractions obtained by cilicic column chromatography were mainly composed of about 93.52% neutral lipid, whereas compound lipid was only 6.48% level. Among the neutral lipid separated by thin layer chromatography, triglyceride was 92.17%, sterol ester, sterol, diglyceride and free fatty acid were 3.53, 2.25, 1.44 and 0.56, respectively. The predominent fatty acids of total and neutral lipids were linoleic acid (59.79-69.37%) and oleic acid (20.04-29.82%), but those of glycolipid and phojspholipid were linoleic acid (29.20-36.04%). The major fatty acids of triglyceride separated from neutral lipid were oleic acid (44.31%), linoleic acid (36.66%) and palmitic acid (12.48%). The salt soluble protein of apple seed was highly dispersible in 0.02M sodium phosphate buffer containing about 1.0M $MgSO_4$, and the extractability of seed protein was 37%, Glutamic acid was the major amino acid in salt soluble protein, followed by arginine and aspartic acid. The eletrophoretic analysis showed three bands in apple seed protein, and the collection rate of the main protein fraction purified by Sephadex G-100 and G-200 was 76.6%. Glutamic acid, aspartic acid and arginine were the major amino acids of the main apple seed protein. The molecular weight for the main protein of the apple seed was estimated to be 45,000.