• Asian-Australasian Journal of Animal Sciences
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• v.19 no.11
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• pp.1546-1550
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• 2006

The purpose of this study was to assess the genetic variation and establish the relationship amongst breeds and strains using 15 chicken specific microsatellite markers. A total of 285 unrelated DNA samples from four Korean native chicken strains (Black strain of Korean native chicken; KL, Red Brown strain of Korean native chicken; KR, Ogol strain of Korean native chicken; KS and Yellow Brown strain of Korean native chicken; KY) and three introduced chicken breeds (F strain of White Leghorn; LF, K strain of White Leghorn; LK, Rhode Island Red; RC and Cornish; CN) were genotyped to estimate within and between breed genetic diversity indices. All the loci analyzed in 15 microsatellite markers showed a polymorphic pattern and the number of alleles ranged from 5 to 14. The polymorphism information content (PIC) of UMA1019 was the highest (0.872) and that of ADL0234 was the lowest (0.562). The expected total heterozygosity (He) within breed and mean number of observed alleles ranged from 0.540 (LF) to 0.689 (KY), and from 3.47 (LK) to 6.07 (KR), respectively. The genetic variation of KR and KY were the highest and the lowest within Korean native strains, respectively. The genetic distance results showed that Korean native chicken strains were separated with the three introduced chicken breeds clustered into another group. The lowest distance (0.149) was observed between the KR and KL breeds and the highest distance (0.855) between the KR and LK breeds. The microsatellite polymorphism data were shown to be useful for assessing the genetic relationship between Korean native strains and other foreign breeds.

• Proceedings of the Korean Biophysical Society Conference
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• 2001.06a
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• pp.31-31
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• 2001

The native strain of serpins (serine protease inhibitors) has been recognized as a mechanism of biological regulation. Indeed, some stabilizing single residue mutations of human $\alpha$$_1$-antitrypsin, a prototype serpin, relieved local strain and caused the loss of inhibitory activity. The native strain of $\alpha$$_1$-antitrypsin is distributed throughout the whole molecule, but the strain that regulates the function directly is highly localized in the regions that appear to be mobilized during complex formation with a target protease.(omitted)

• Korean Journal of Poultry Science
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• v.45 no.3
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• pp.175-182
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• 2018

The carcass and meat quality of new native chicken strains (A, C, and D) being developed in the Golden Seed Project for Samgyetang were compared with a commercial native chicken (Hanhyup No. 3, H) and Baeksemi (white semi broiler, W) strains. In total, 250 male chicks were raised under the same feeding and raising conditions for 5 weeks. After slaughter, the carcass weight and percentage yield of parts from each strain were measured and the physicochemical quality traits (general composition, color values, fatty acid composition, and sensory evaluation) of breast muscles were comparatively analyzed. The carcass weight (875.10 g) of the W strain was significantly heavier than that of the other native chicken strains, while that of A strain (537.54 g) was the lowest. The percentage yield of breast meat was also higher in the W strain than in the other strains. The fat content of W strain was higher than that of the other native chicken strains. The new native chicken strains (A, C, D) had higher contents of linoleic acid (C18:2) than the H strain. The A and D strains especially showed relatively high content of arachidonic acid (C20:4), a characteristic fatty acid in native chicken meats. On the other hand, the fatty acid composition of C strain was similar to that of the W strain. This study provides important information on specific quality characteristics than can be used to select new native chicken lines for breeding program.

• Proceedings of the Korean Biophysical Society Conference
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• 2002.06b
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• pp.30-30
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• 2002

The native forms of common globular proteins are in their most stable state but the native forms of plasma serpins (serine protease inhibitors) show high-energy state interactions. The high-energy state strain of a ${\alpha}$$_1$-antitrypsin, a prototype serpin, is distributed throughout the whole molecule, but the strain that regulates the function directly appears to be localized in the region where the reactive site loop is inserted during complex formation with a target protease.(omitted)

• Korean Journal of Agricultural Science
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• v.39 no.1
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• pp.53-60
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• 2012

This work was conducted to evaluate the laying performance of Korean Native Ducks (KND) Pure-Line (PL). A total of 400 female pullets were hatched from PL to keep in National Institute of Animal Science, Korea. Twenty weeks old PL female ducks were divided into 4 groups (5 replications/group, 20 head/replications). Four groups were compared in a $2{\times}2$ factorial arrangement with strain (White strains, WW; Celadon strains, CC) and house type (flat house, cage house). On first egg laying day, CC strain laid eggs earlier compared to WW strain (P<0.01), but there was no significant difference between flat and cage house. Egg weight (EW) and body weight (BW) at first egg laying day have no difference among strains and houses. BW of CC strain was higher than WW strain at the age of 30 week (P<0.01). Weekly feed intake (FI) have no difference between flat and cage house, but FI of WW strain was high compared to CC strain during 20~30 weeks. There was no significant difference on EW between CC and WW strains, but EW was low at flat house compared to cage house (P<0.05). Weekly egg productions of WW strain and flat house were lower than CC strain and cage house, respectively (P<0.01). Finally, These results can provide the information that needed to introducing new strains.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.42-42
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• 1999

Metastability in the native form of proteins has been recognized as a mechanism of biological regulation. The strained native structure of serpins (serine proteinase inhibitors) is a typical example. The native strain of serpins is considered to be crucial to their physiological functions, such as plasma proteinase inhibition, hormone delivery, Alzheimer filament assembly, and extracellular matrix remodeling.(omitted)

• Korean Journal of Poultry Science
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• v.46 no.4
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• pp.255-262
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• 2019

The micronutrients and flavor compounds of three new native chicken strains (A, C, and D) being developed in a breeding program (Golden Seed Project) were compared with a commercial native chicken strain (H) and the Baeksemi (W, white semi broiler). After 100 male chicks in each strains were reared for 5 weeks, the breast muscles from randomly selected 40 birds were analyzed at 8 replications. Native chicken strain A had greater amounts of α-tocopherol and α-tocotrienol compared with strain W. Native chicken strains showed higher contents of vitamin B₁₂ than Stain W. Stain H strain had the highest values of cholesterol content and strain D did the lowest. There was no different content of most minerals between native chickens (A, C, D, and H) and W, but Cu were more contained in native chicken strains compared with W. In terms of nucleotide-related flavor compounds, Stain A had the lowest content of hypoxanthine and strain D had highest inosine monophosphate. Native chicken strains had higher contents of umami-related free amino acids (glutamate and aspartate) than W. Among native chickens, strain A had more amounts in the contents of taurine, tasty flavor compounds, and certain vitamins, despite of the relatively low growth productivity. This result will provide information to select a strain with characteristic meat quality in a chicken breeding program.

• Proceedings of the Korean Biophysical Society Conference
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• 1997.07a
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• pp.39-39
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• 1997

Native strain of inhibitory SERPINS (Serine protease inhibitors) is thought to be used in the facile conformational switch to play biological regulation. Many heat stable variants of $\alpha$$_1$-antitrypsin, a prototype of inhibitory serpins, increased their stability by reducing the native strain.(omitted)

• Korean Journal of Poultry Science
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• v.25 no.4
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• pp.177-183
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• 1998

A feeding trial was conducted to investigate the performance of various Korean Native Chickens (KNC) for 64 weeks. Eight hundreds and ten KNC one-day birds were arranged to three strains, Dark Brown(D), Light Brown(L) and Black(B). Each strain had three replicates of 90 birds a replicate. Birds fed same diet with Korean standard feeding. Data were obtained growing performance to 20 week of age and laying performance from twenty one to sixty four week. During the growing stage from hatch to 20 week of age, there were not significant difference to three strains on viability, body weight and feed intake. L strain tended to be earlier 50％ egg production day than that of other strains, but was not significantly different. Egg production of L strain was the highest of strains. It showed significantly higher egg production compared to that of D strain(P<0.05), but was not statistically different from that of B strain. Laying peak period was between 28 to 32 week of age in all strains, Egg weight was heavier in D strain(P<0.05). Feed intake was the same as 105g, and feed conversion improved in L strain(P<0.05). There were not difference on interior egg and eggshell quality by strains although eggshell thickness improved slightly in D strain. Fertility of D strain was the highest compared to others(P<0.05) regardless laying stages. Hatchability was not influenced by strains at 39 weeks old, but was significantly higher in B strain at 62 week of age(P< 0.05). The results of this experiment indicated that KNC 3 strains were not effect on egg production, feed intake and feed conversion ratio.

• BMB Reports
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• v.33 no.5
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• pp.379-384
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• 2000

The native conformation of serpins (serine protease inhibitors) is strained. Upon cleavage of the reactive center loop of serpins by a protease, the amino terminal portion of the cleaved loop is inserted into the central ${\beta}-sheet$, A sheet, as the fourth strand, with the concomitant release of the native strain. We questioned the role of protease in this conformational switch from the strained native form into a stable relaxed state. Chemical cleavage of the reactive center loop of ${\alpha}_1-antitrypsin$, a prototype serpin, using hydroxylamine dramatically increased the stability of the serpin. A circular dichroism spectrum and peptide binding study suggests that the amino terminal portion of the reactive center loop is inserted into the A sheet in the chemically-cleaved ${\alpha}_1-antitrypsin$, as in the enzymatically-cleaved molecule. These results indicate that the structural transformation of a serpin molecule does not require interaction with a protease. The results suggest that the serpin conformational switch that occurred during the complex formation with a target protease is induced by the cleavage of the reactive center loop per se.