• Applied Microscopy
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• 제19권2호
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• pp.74-84
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• 1989

인삼 종자의 배유조직에서 Tris 완충액 가용성 저장단백질을 추출한 후 전기 영동적 분석으로 분리하여 $SP_{1}$(MW=160,000)과 $SP_2$(MW=70,000)의 두가지 저장단백질을 정제하였다. 이 두가지 저장단백질을 항원으로 사용하여 토끼에 피하주사하여 항체를 얻었으며, 이 항체를 이용하여 면역 세포화학적 금입자표지법을 실시한 결과, $SP_1$과 $SP_2$ 모두 구형의 protein body내에 산재하여 있음을 확인되었으며, globoid에는 이러한 두가지 단백질중 어느 것도 함유되어 있지 않는 것으로 나타났다. 또한 각각의 protein body에 함유된 $SP_1$과 $SP_2$의 상대적 함량에는 서로 차이가 있음이 확인되었다.

• 한국식품영양과학회지
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• 제22권6호
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• pp.763-770
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• 1993

To investigate the quality changes during frozen storage, top shell, Omphalius pfeifferi capenteri, was stored at -18$^{\circ}C$, -$25^{\circ}C$ and -3$0^{\circ}C$ immediately after shelling and water holding capacity, protein composition and histological features were examined with the lapsed period of the storage. During the storage period, amount of free drip was increased with higher frozen temperature and longer frozen period, but with the longer storage period, the lower water holding capacity was observed. The extractability and composition of muscle protein, sarcoplasmic protein and stroma protein were rather stable regardless of frozen temperature and frozen storage period. However, the extractability of myofibrillar protein was decreased with higher frozen temperature and longer frozen storage period. On the changes of muscle tissue structure, following points were observed. 1) In the muscle tissue structure of fresh sample, fine muscle fiber was closely distributed all over the tissue regardless of cross and longitudinal section. 2) In tissue structure under frozen state, it was observed that ice crystals apparently grew with the higher storage temperature. Empty spaces between muscle bundles which wee formed by aggregations of muscle fiber were observed after 3 months storage at -18$^{\circ}C$ . 3) Tissue structure in thawed state was restored satisfactorily after 1 month storage regardless of storage temperature. After 3 months storage at -3$0^{\circ}C$, muscle tissue was well restored, but at -18$^{\circ}C$, empty spaces were apparent due to incomplete restoration.

• 한국동물학회지
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• 제33권3호
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• pp.346-353
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• 1990

두 종류의 저장단백질이 매미나방의 발생기간동안 혈림프와 지방체에서 발견되었다. SPl은 분자량이 440,000이며 6개의 동일한 subunit으로 구성되어 있다. 또한 SPl은 당과 지질을 함유한 복합단백질이며 그 등전점은 6.2이었다. SPl은 암수 모두 종령기간동안 비슷한 고농도를 보여 주었지만 번데기시기에는 암수가 상이한 패턴을 보여주었다. 즉 SPl은 수컷에서 점진적 감소를 보여준 반면 암컷에서는 점진적 증가를 보여주었다. SPl은 면역학적으로 난황단백질과 동일성을 보여 주었고, 미국흰불나방과 꿀벌부채나방의 저장단백질과 부분적인 동질성을 보여주었다.

• 한국축산식품학회지
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• 제20권4호
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• pp.320-325
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• 2000

The diet had an effect(P<0.05) on the nutritional contents of ostrich meat during 4 month of frozen storage. As frozen storage increased up to 4 months, pJ, water holding capacity(WHC) and myofibrillar protein solu-bility($\mu$g/$\mu$l) were reduced (P<0.05), how-ever, increased drip loss(DL, %) was found in ostrich muscle from forage fed ostriches, This study suggests that forage fed ostriches, This study suggests that frozedn storage(-2$0^{\circ}C$)up to 4 months in ostrich FCL muscle (outside strip)could be reduced protein functionality, due to increase in DL. decrease in WHC, and markedly decrease in myofibrillar protein solubility($\mu$g/$\mu$l).

• Journal of Plant Biology
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• 제39권2호
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• pp.123-126
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• 1996

The pattern of seed storage protein, vicilin, deposition and site of intracellular localization was examined in cotyledon cells of pea (Pisum sativum) seed using the immunocytochemical methods. The vicilin was confined to the cisternae fo the rough endoplasmic reticulum and dictyosome as well as protein granules newly formed in rough endoplasmic reticulum. Vacuolar protein deposites and protein bodies were also labelled by gold particles. After small protein bodies were formed in the rough endoplasmic reticulum, they were transported to large protein bodies and then fused together. Electron dense protein granule, elaborated in the dictyosome, appears to be transported from dictyosome to protein body. A few unlabelled protein granules seem to be accumulated in other type of proteins than vicilin.

• 한국동물학회지
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• 제29권1호
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• pp.1-12
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• 1986

누에의 變態期 동안 貯藏蛋白質의 出現과 번데기 시기동안 각 組織에 따른 貯藏蛋白質의 分布를 살펴보기 위해 電氣泳動法, 免疫學的 方法 및 column chromatography法을 使用하였다. 혈림프의 貯藏蛋白質은 2개로 區分이 되었고, 5령 初期부터 出現하고 있으며 지방체 단백질과도 동일한 전기영동상의 移動度를 갖고 있다. 이의 量的 變化는 終令期에는 혈림프에서 높은 濃度를 유지하다. 　化後에는 脂肪體에 축적이 되는 경향을 나타내며 특히 저장단백질-2가 암수에서 모두 두드러진 저장단백질의 양상을 보이고 있다. 이러한 貯藏蛋白質은 종령 末期에는 큐리클 단백질 형성에도 관여하는 것 같으며 번데기에는 中腸도 일시적으로 저장단백질을 저장하는 것 같다. 또한 貯藏蛋白質中 저장단백질-2는 vitellogenin과 정기영동 및 면역학적으로 동일한 이동도를 나타내고 있으며 특히 번데기시기동안 卵黃蛋白質의 항체에 대해 항원-항체반응을 나타내고 있어 卵形成過程에도 밀접하게 관여하는 것 같다.

• 한국축산식품학회지
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• 제37권2호
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• pp.254-263
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• 2017

The inhibition effect of persimmon peel extracts (PPE) (0.05(PPE-0.05), 0.1(PPE-0.1), and 0.2 g(PPE-0.2) per meat sample) on lipid and protein oxidation of pork patties during chilled storage for 12 days were investigated and compared to ascorbic acid (As-0.05) and butylhydroxytoluene (BHT) (BHT-0.01). The meat samples treated with PPE had greater (p<0.05) $a^*$ values comparing control in raw pork patties meat from day 4 of storage. The addition of PPE at all concentrations on meat samples effectively inhibited the formation of oxidation products as shown by decreasing conjugated dienes (CD), peroxide values (POVs), thiobarbituric acid reaction substances (TBARS), and carbonyl content during chilled storage for 12 d. The PPE-0.2 and BHT-0.01 had the lowest in decrease rate of free thiol content (0.24 and 0.22 times) during chilled storage. Therefore, results of this study suggest that PPE can be considered a potential antioxidant against lipid and protein oxidation of raw meat products.

• International Journal of Industrial Entomology and Biomaterials
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• 제2권2호
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• pp.161-166
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• 2001

The storage proteins of the mulberry longicorn beetle, Apriona germari Hope, were purified and characterized. Three kinds of storage protein (SP1, SP2 and Sp3) were purified from the last instar larval hemolymph of A. germari by the FPLC techniques, anion exchange chromatography and gel permeation chromatography. The SP1, SP2 and SP3 have a native molecular weight of 480, 440 and 420 kDa, respectively. In the SDS-polyacrylamide gel electrophoresis analysis, these storage proteins are composed of a single protein subunit with molecular weight of 90, 85 and 80 kDa, respectively. This result showed that the storage proteins are hexameric protein. The SP1 and SP2 were stained with Schiffs reagent, but SP3 was not stained. It can be assumed that SP1 and SP2 are glycoprotein. Western blot analyses using the each of polyclonal antiserum against purified SP1, SP2 and SP3 showed that the three antibodies reacted with the each of SP bands, respectively. Also, antibodies against SP1 and SP3 cross-reacted with the SP3 and SP1, respectively. However, SP2 was not cross-reacted with these two antibodies. Also, antiserum against SP2 did not cross-reacted with the SP1 and SP3.

• 한국잠사곤충학회지
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• 제41권2호
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• pp.75-81
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• 1999

The storage protein-like protein has been purified from the 5th instar larval haemolymph of the Chinese osk silkwom, Antheraea pernyi, and the preparation was shown to be homogeneous by 7.5% native-PAGE. The molecule was consisted of a single subunit with a molecular weight of 80K, but the number of the subunits was not determined. The protein was defied as glycoprotein by Schiff's regent stining. Rabbit antibody prepared against the purified protein crotein crossreacted with the 5th instar larval haemolymph proteins of Antheraea pernyi and antheraea yamamai, but not with those of Bombyx mori and Bombyx mandarina.

• Asian-Australasian Journal of Animal Sciences
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• 제32권2호
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• pp.265-273
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• 2019

Objective: Terminalia arjuna plant, specially its leaves, bark, and roots, are widely used in traditional herbal medicine due to presence of bioactive components and being a rich source of natural antioxidants. But its fruit has not been used for any such purposes despite its potential to retard oxidation. Hence, the antioxidant potential of Arjuna fruit extract (AFE) in retarding lipid and protein oxidation of raw ground pork was evaluated during refrigerated storage for 9 days. Methods: The AFEs were prepared using different solvents viz. ethanol (EH), water, ethanol: water (60:40) and methanol:hot water (60:40). The AFEs were analysed for total phenolic content (TPC), 2, 2-diphenyl-1-picrylhydrazyl radical scavenging activity and reducing power. Water extract (WE) and ethanol-water extract (EH-WE) were selected and incorporated at 1.0% into freshly minced pork meat and compared with a synthetic antioxidant, in retarding lipid and protein oxidation during storage. Results: The TPC in AFEs using different solvents ranged from 11.04 to 16.53 mg gallic acid equivalents/g and extracts exhibited appreciable scavenging activity ranging from 50.02% to 58.62%. Arjuna extracts significantly (p<0.05) improved the colour score of meat samples by reducing the formation of metmyoglobin during storage. Both the AFEs (WE and EH-WE) significantly (p<0.05) lowered the thiobarbituric acid reactive substances value, peroxide formation and formation of protein carbonyls in raw pork than control sample during storage. Upon sensory evaluation of all samples, it was found that AFE treatment could prolong the storage period of meat samples, without influencing the colour and odour score, up to 6 days. Conclusion: AFEs used at 1% improved the oxidative stability, colour and odour score and prolonged the refrigerated shelf life of ground pork up 6 days. Therefore, AFE could be explored as an alternative natural antioxidant in retarding lipid and protein oxidation in meat products.