• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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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.

• Applied Microscopy
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• v.19 no.2
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• pp.74-84
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• 1989

Buffer soluble storage proteins of ginseng seed have been localized by electron microscopy using post-embedding immunocytochemical gold labelling technique. Major components of the storage proteins were revealed to be storage protein-1($SP_{1}$, MW 160,000) and storage protein-2($SP_{2}$, MW 70,000). Both of the storage proteins are glycoproteins. Anti-$SP_{1}$ and anti-$SP_{2}$ from rabbit, against $SP_1$ and $SP_2$, respectively, reacted on sections of ginseng endosperm tissue embedded in Spurr's epoxy resin. The rabbit antibodies were visualized indirectly by reaction with protein A labelled with colloidal gold. Both storage proteins were found to be accumulated together in the same protein bodies, but their relative contents are not equal.

• Korean Journal of Environmental Agriculture
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• v.27 no.4
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• pp.456-459
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• 2008

Quality of rice grain changes during dry storage with internal physiological changes and external injury by organism. Storage rice changes by condition with respiration via variable temperature, hydrolysis enzyme reaction, lipid peroxidation occurs with change of palatability. During dry storage, physiological change with protein variation pattern was examined by image analysis on proteomic technology. Analysis revealed that protein activity had no change store at room temperature and store at $40^{\circ}C$, but decreased store at $60^{\circ}C$. Analysis of variable hydrophobic protein pattern revealed that protein activity of beta-tubulin, protein disulfide isomerase, vacuolar ATPase b subunit, globulin was not significantly decreased all dry and store condition. However, heat shock protein 70, and glutathione transferase was significantly decreased when rice dried at $60^{\circ}C$ compared with room temperature and $40^{\circ}C$ dry condition.

• Animal cells and systems
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• v.5 no.1
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• pp.85-90
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• 2001

Yolk platelets, one of the main food stores in the embryonic development, are composed of proteins. However, little is known about the identity of proteins utilized at certain stages of embryogenesis. In this study, we followed the fates of embryonic storage proteins by using an anti-polyubiquitin monoclonal antibody (mAB) as a probe. The mAb recognized the major storage proteins of Drosophila, Xenopus and chicken eggs. In the Drosophila embryo, the mAb-reactive 45-kDa protein was not used until stage 11 but was used up at stage 16 when the embryo completed segmentation. In the Xenopus embryo, the mAb-reactive 111 kDa protein was mostly utilized between stages 42 and 45 implying that the protein might be an energy source used just prior to feeding on food. By N-terminal sequencing the storage protein of Xenopus embryo was identified as a lipovitellin 1. This study confirms that storage proteins are used almost simultaneously at certain stages of embryogenesis and that vitellogenin 1 is the last storage protein in Xenopus embryogenesis.

• Korean journal of food and cookery science
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• v.24 no.3
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• pp.304-311
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• 2008

This study examined Jeung-pyun(JP) Retrogradation in samples containing 3% whole protein, 7S protein, or 11S protein(w/w) that were stored at $4^{\circ}C$ for 6, 12, 24 and 72 hr. Rheometery and differential scanning calorimetry(DSC) were used in the analysis. The pH of the dough decreased during the fermentation process, but it increased after steaming. The JP prepared with soybean protein isolate(SPI) had higher pH than the control group. During storage the textural characteristics of the JP showed effects according to the additions of SPI. After 6 hr of storage, the JP samples containing soybean flour, whole protein, 7S protein, and 11S protein had lower hardness valuse. From 4 hr to 12 hr, higher springiness values were found in the samples containing whole protein, 7S protein and 11S protein. At 0 hr, the control group had the highest cohesiveness value, but after 24 hr it presented the lowest value. For gumminess, after 6 hr of storage, the control group offered the lowest value. Whereas after 12 hr of storage the whole protein group showed the highest value, and at 24 hr, the whole protein, 7S protein, and 11S protein groups had higher values. According to the DSC results, the 11S protein group had lower enthalpy values(${\bigtriangleup}H$) suggesting that adding 11S protein to JP might improve starch retrogradation. After 72 hr of storage, the control group had the highest onset temperature($T_{o}$) and peak temperature($T_{p}$) whereas the 7S and 11S protein JP samples had higher conclusion temperatures($T_{c}$). Therefore, based on the different analysis result between the control and treatment groups, the addition of SPI to Jp had effects on retrogradation.

• Food Science of Animal Resources
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• v.20 no.4
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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).

• Applied Microscopy
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• v.29 no.4
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• pp.499-509
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• 1999

Accumulations of the storage proteins in protein storage vacuole and the differentiation of protein bodies from protein-filled ER in developing pea cotyledons have been investigated using conventional and immunoelectron microscopy. To improve the fixation quality, single cells separated enzymatically from sliced cotyledons were used. At early stages of seed development osmiophilic protein accumulates in rER lumen were observed quite often. This protein-filled ER cisternae were differentiated into cytoplasmic protein bodies at late stage by the process called terminal dilations which have been considered a principal route of the formation of cytoplasmic protein bodies somewhat later in seed maturation. Immunocytochemical labellings of the vicilin and legumin show that presence of vicilin on both of the cytoplasmic PB and PD, but limited presence of legumin only on the cytoplasmic PB at intermediate stage of seed development. Immunogold labellings of Bip, ER retention protein, were observed on the inner periphery of protein deposits in protein storage vacuole. This result was regarded that Bip can recognize and retrieve misfolded protein during active accumulation of storage protein to the PD in PSV.

• Journal of Plant Biology
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• v.39 no.2
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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.

• Journal of Plant Biotechnology
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• v.8 no.1
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• pp.1-8
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• 2006

The differential response of soybean cultivars with or without sulfur (S) application was observed under fold conditions. Plant biomass decreased by sulfur deficiency but the reduction was less in Bragg variety about 26 % relative to the control than other ones over 45%, probably due to less reduction in loaves and pods. The photosynthetic rate of Bragg cultivar was also unaffected by the absence of sulfur application while it depressed in other lines. Soybean cultivars were compared in terms of storage protein, protein quality and biomass production by application of sulfur nutrition. The storage protein concentration tended to decrease without sulfur application in all the cultivars, however the differential response of protein quality only by 11S/7S ratio to sulfur nutrition status was observed: For instance, Bragg cultivar had higher biomass and protein production but protein quality decreased at sulfur deficiency. On the other hand, biomass and protein production in other cultivars remained louver at sulfur deficiency but protein quality differed genetically in spite of sulfur nutrition status. These results suggest that the response of soybean to sulfur nutrition is controlled by genotypic difference and sulfur supply status.

• Journal of Sericultural and Entomological Science
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• v.41 no.2
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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.