• 한국동물학회지
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• 제18권1호
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• pp.27-40
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• 1975

dbcAMP와 theophylline이 난자의 성숙을 억제하는 기작과 난자내 glycogen 함량과의 관계를 밝혀보기 위하여 실험한 결과는 다음과 같다. 1. 생쥐 여포난자의 PAS 양성물빌은 glycogen이며 핵의 성숙분열이 진행됨에 따라 glycogen의 함량은 감소한다. 2. dbcAMP나 theophylline에 의해 핵의 성숙이 억제된다 하더라도 난자내의 glycogenolysiss는 촉진된다. 이에 반해 핵분열이 일어나지 않은 난자는 배양이 진행되더라도 glycogen을 그대로 유지하고 있다. 일단 dbcAMP나 theophylline에 의해 성숙이 억제되었던 난자가 성숙과정에 들어가려면 다시 glyconeogenesis가 일어나 세포질내의 glycogen의 양이 회복하며 이때의 glycogen은 핵성숙과 더불어 소모된다. 3. Glycogen의 회복은 배양액내의 glucose 유무에 관계없이 이루어지며 따라서 이는 난자내 glucose 혹은 다른 전구물질에 의해 이루어지리라고 추측된다. 4. 결국 dbcAMP나 theophylline은 난자내 cAMP의 양을 증가시켜 glycogen의 소모를 일으키는 것으로 생각되며, glycogenolysis와 난자의 핵 성숙과정이 별개로 진행되기는 하지만 성숙의 요건은 일정량 이상의 glycogen이 함유되어 있어야 한다는 것을 알게되었다.

• 한국동물학회지
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• 제19권1호
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• pp.1-6
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• 1976

생쥐 여포난자를 배양하면서 감수 분열 각 단계에서 난자내 glycogen함량의 변화를 Microspectrophotometer를 사용하여 조직화학적방법으로 조사하였다. 난자의 성숙이 진행됨에 따라 PAS반응은 감소하며, 퇴화중인 난자의 glycogen함량은 현저히 적었다. 난자내 glycogen은 난자의 성숙을 유도하는 역활을 나타내며, 핵막이 붕괴하기 전에 glycogen이 소모되면 난자의 퇴화를 일으킨다. 본 실험의 결과 난자내 glycogen은 감수분열의 진행에 있어서 중요한 요인이 됨을 알 수 있었다.

• 한국식품영양과학회지
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• 제27권6호
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• pp.1173-1176
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• 1998

Glycogen synthetase[EC 2.4.1.21] in E. coli B was isolated and purified by sonication, ultracentri fugation, DEAE cellulose chromatography and gel chromatography. In the case of using glycogen or maltotriose as a primer in the enzyme reaction, 64% and 23.7% of labelled ADP glucose were incorporated into primer, respectively. 8.1% of labelled ADP glucose was polymerized into glycogen in enzymatic reaction without a primer.

• BMB Reports
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• 제35권3호
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• pp.283-290
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• 2002

The glycogen-associated protein phosphatase (PP1G/$R_{GL}$) may play a central role in the hormonal control of glycogen metabolism in the skeletal muscle. Here, we investigated the in vivo epinephrine effect of glycogen metabolism in the skeletal muscle of the wild-type and $R_{GL}$ knockout mice. The administration of epinephrine increased blood glucose levels from 200±20 to 325±20 mg/dl in both wild-type and knockout mice. Epinephrine decreased the glycogen synthase -/+ G6P ratio from 0.24±0.04 to 0.10±0.02 in the wild-type, and from 0.17±0.02 to 0.06±0.01 in the knockout mice. Conversely, the glycogen phosphorylase activity ratio increased from 0.21±0.04 to 0.65±0.07 and from 0.30±0.04 to 0.81±0.06 in the epinephrine trated wild-type and knockout mice respectively. The glycogen content of the knockout mice was substantially lower (27%) than that of both wild-type mice; and epinephrine decreased glycogen content in the wild-type and knockout mice. Also, in Western blot analysis there was no compensation of the other glycogen targeting components PTG/R5 and R6 in the knockout mice compared with the wild-type. Therefore, $R_{GL}$ is not required for the epinephrine stimulation of glycogen metabolism, and rather another phosphatase and/or regulatory subunit appears to be involved.

• Journal of Microbiology
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• 제39권1호
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• pp.24-30
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• 2001

In addition to effecting the catalysis of sugar uptake, the bacterial phosphoenolpyruvate::sugar phosphotransferase system regulates a variety of physiological processes. In a previous paper [Seok et al.,(1997) J. Biol. Chem. 272, 26511-26521], we reported the interaction with and allosteric regulation of Esiherichia coli glycogen phosphorylase activity by the histidine-containing phosphocarrier protein HPr in vitro. Here, we show that the specific interaction between HPr and glycogen phosphorylase occurs in vivo. To address the physiological role of the HPr-glycogen phosphorylase complex, intracellular glycogen levels were measured in E. coli strains transformed with various plasmids. While glycogen accumulated during the transition between exponential and stationary growth phases in wildtype cells, it did not accumulate in cells overproducing HPr or its inactive mutant regardless of the growth stage. From these results, we conclude that HPr mediates crosstalk between sugar uptake through the phosphoenolpyruvate:sugar phosphotransferase system and glycogen breakdown. The evolutionary significance of the HPr-glycogen phosphorylase complex is suggested.

• 한국미생물·생명공학회지
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• 제46권1호
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• pp.29-39
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• 2018

Vibrio vulnificus needs various responsive mechanisms to survive and transmit successfully in alternative niches of human and marine environments, and to ensure the acquisition of steady energy supply to facilitate such unique life style. The bacterium had genetic constitution very different from that of Escherichia coli regarding metabolism of glycogen, a major energy reserve. V. vulnificus accumulated more glycogen than other bacteria and at various levels according to culture medium and carbon source supplied in excess. Glycogen was accumulated to the highest level in Luria-Bertani (3.08 mg/mg protein) and heart infusion (4.30 mg/mg protein) complex media supplemented with 1% (w/v) maltodextrin at 3 h into the stationary phase. Regarding effect of carbon source, more glycogen was accumulated when maltodextrin (2.34 mg/mg protein) was added than when glucose or maltose (0.78.1-14 mg/mg protein) was added as an excessive carbon source to M9 minimal medium, suggesting that maltodextrin metabolism might affect glycogen metabolism very closely. These results were supported by the analysis using the malP (encoding a maltodextrin phosphorylase) and malQ (encoding a 4-${\alpha}$-glucanotransferase) mutants, which accumulated much less glycogen than wild type when either glucose or maltodextrin was supplied as an excessive carbon source, but at different levels (3.1-80.3% of wild type glycogen). Therefore, multiple pathways for glycogen metabolism were likely to function in V. vulnificus and that responding to maltodextrin might be more efficient in synthesizing glycogen. All of the glycogen samples from 3 V. vulnificus strains under various conditions showed a narrow side chain length distribution with short chains (G4-G6) as major ones. Not only the comparatively large accumulation volume but also the structure of glycogen in V. vulnificus, compared to other bacteria, may explain durability of the bacterium in external environment.

• Journal of Ginseng Research
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• 제18권2호
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• pp.102-107
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• 1994

When at liver homogenates were incubated with 1mM $CCl_4$ for five min, glycogen level was decreased, while treatment with protein fraction $G_4$ increased the glycogen level. In addition $G_4$ inhibited the phosphorylation of 34 KD and 118 KD polypeptides induced by $CCl_4$. These protein were more strongly phosphorylated by $Ca^{2+}$/calmodulin-dependent kinase than by C-kinase. Since 34 KD polypeptide was solely phosphorylated by NaF (50mM), an inhibitor of both glycogen syntheses and phosphoprotein phosphates, it is inferred that 3 KD polypeptide is glycogen synthase-likd protein. Because glycogen synthesis is inhibited by phosphorylation of $Ca^{2+}$-dependent glycogen syntheses, it is suggested that $G_4$ increased liver glycogen level by inhibiting phosphorylation of 34 KD polypeptide which is thought to glycogen syntheses-like protein.

• 대한수의학회지
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• 제36권3호
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• pp.521-529
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• 1996

In an effort to obtain basic data of carbohydrate metabolism during spermiogenesis of the sexually-matured Jindo dog, the glycogen distribution in the testis was investigated by light and transmission electron microscopy. Periodic acid thiocarbohydrazide silver proteinate physical development(PA-TCH-SP-PD) staining method provided better results in the detection of glycogen granules from Sertoli cells and germ cells than the periodic acid schiff(PAS) staining method did. Pre-treatment of the tissue sections with ${\alpha}$-amylase elicited a significant decrease in PA-TCH-SP-PD stained granules, which suggested that the stained granules were of glycogen origin. High concentration of the glycogen granules were observed in the Sertoli cells, especially in its column, sheet-like processes, club-like processes, and tubular processes. The glycogen granules were unevenly distributed in some Sertoli cell columns. These results strongly indicated that the Sertoli cells of Jindo dogs showed vigorous activity of carbohydrate metabolism.

• Journal of Yeungnam Medical Science
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• 제5권2호
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• pp.79-86
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• 1988

Sprague-Dawley중 흰쥐에게 $^{14}C$-glucose가 들어있는 glucose용액을 경구 투여한 후 특성이 다른 골격근에서 투여 glucose가 glycogen으로 합성된 양과 운동부하가 이에 미치는 효과를 관찰한 본 연구 결과를 요약하면 다음과 같다. Glucose 경구투여 후 위장관에서의 흡수율은 운동부하군 및 대조군 모두 30분에 55% 정도였고 90분후에는 70% 가량이 흡수되었다. 투여 glucose로부터 유래된 골격근 glycogen 합성량은 양군 모두 SOL에서 가장 높았으며 WV가 가장 낮았다. 운동부하군이 대조군에 비하여 glycogen 합성량이 많았으며 특히 SOL, RV에서 현저히 높았다. 운동부하군에서 투여 glucose로부터 합성된 glycogen의 양이 90분후에는 SOL, RV 그리고 EDL에서는 대조군보다 월등히 많았으나 WV에서는 차이가 없었으며 30분경에는 SOL만이 유의하게 높았다. 투여 glucose에서 유래한 glycogen 합성속도는 운동부하군에서 WV를 제외한 모든 근육에서 초기 30분보다 후반 60분이 월동이 빨랐으나 SOL을 제외한 대조군과 WV는 처음 30분동안에 대부분의 glycogen이 합성되었다. 간장에서는 투여 glucose로부터 합성된 glycogen양은 양군 모두에서 초기 30분동안에는 합성량이 미미했으나 운동부하군의 90분동안에는 30분에 비하여 무려 20여배의 증가를 보였다.

• 한국미생물·생명공학회지
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• 제46권3호
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• pp.194-200
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• 2018

Glycogen plays important roles in bacteria. Its structure and storage capability have received more attention recently because of the potential correlations with environmental durability and pathogenicity. However, the low level of intracellular glycogen makes extraction and structure characterization difficult, inhibiting functional studies. Bacteria grown in regular media such as lysogeny broth and tryptic soy broth do no accumulate large amounts of glycogen. Comparative analyses of bacterial media reported in literature for glycogen-related studies revealed that there was no consistency in the recipes reported. Escherichia coli $DH5{\alpha}$ is a convenient model organism for gene manipulation studies with respect to glycogen. Additionally, M9 minimal salts medium is widely used to improve glycogen accumulation, although its composition varies. In this study, we optimized the M9 medium by adjusting the concentrations of itrogen source, tryptone, carbon source, and glucose, in order to achieve a balance between the growth rate and glycogen accumulation. Our result showed that $1{\times}M9$ minimal salts medium containing 0.4% tryptone and 0.8% glucose was a well-balanced nutrient source for enhancing the growth and glycogen storage in bacteria. This result will help future investigations related to bacterial physiology in terms of glycogen function.