• Asian-Australasian Journal of Animal Sciences
• /
• 제31권6호
• /
• pp.905-913
• /
• 2018

Objective: To evaluate the effects of L-lysine (Lys)/L-arginine (Arg) on lipid and protein oxidation of emulsion sausage during storage and its possible mechanism. Methods: Four samples were prepared based on the presence or absence of additional sodium isoascorbate, Lys, or Arg: sample A (control), sample B (0.05 g of sodium isoascorbate), sample C (0.4 g of Lys), and sample D (0.4 g of Arg). Peroxide value (POV), thiobarbituric reactive substances (TBARS), protein carbonyls and thiols were measured. 2,2-Diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radical-scavenging, ferrous ion-chelating ability were also measured. Results: Compared with the control, the sample treated with sodium isoascorbate, Lys or Arg had significantly lower POV during the initial 20 days, TBARS during the initial 15 days. Protein carbonyls were significantly lower compared Sample B, C, and D with A during the later storage (10 to 25 days); basically, protein thiols became lower during storage when the samples were treated with sodium isoascorbate, Lys, or Arg. Both Lys and Arg had weak reducing power but strong ferrous ion-chelating activity and DPPH radical- and hydroxyl radical-scavenging activity. Conclusion: Both Lys and Arg effectively inhibited the oxidation of lipids and proteins in emulsion sausage by scavenging free radicals and chelating ferrous ions. The results obtained may be favorable for the prevention of lipid and protein oxidation during processing and storage of meat products.

• 한국생물공학회:학술대회논문집
• /
• 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
• /
• pp.688-691
• /
• 2000

Ferritin, an iron-storage protein, is found in bacteria and some animal tissues such as liver, spleen, and bone marrow. It is more effective and causes less side reactions than the traditional ferrous sulfate, and thus has been used primarily to treat iron deficiency in pregnancy anaemia. Currently, the ferritin extracted from the bovine and equine spleens are sold as a commercial product. Its market is estimated as several hundreds of million US dollars. However, because of the recent warnings against the viral diseases of animal origins such as mad cow disease, a safer ferritin is sought after. Our research team has successfully developed a production process for recombinant human ferritin. Its expression titer from yeast is high enough to be economically viable, and its particle formation characteristics are as effective as well.

• Reproductive and Developmental Biology
• /
• 제39권4호
• /
• pp.117-125
• /
• 2015

Iron is required for cell viability but is toxic in excess. While the iron-mediated malfunction of testicular cells is well appreciated, the underlying mechanism(s) of this effect and its relationship with fertility are poorly understood. Ferritin is a ubiquitous intracellular protein that controls iron storage, ferroxidase activity, immune response, and stress response in cells. Ferritin light chain protein (FTL) is the light subunit of the Ferritin. Previously, we had identified the FTL in bovine spermatozoa following capacitation. In present study, to investigate the role of Ferritin in sperm function, mice spermatozoa were incubated with multiple doses (1, 10 and $100{\mu}M$) of sodium nitroprusside (SNP), an iron donor. SNP was increased Ferritin levels in a dose-dependent manner. The Ferritin was detected on the acrosome in spermatozoa by immunocytochemistry. Short-term exposure of spermatozoa to SNP increased tyrosine phosphorylation and the acrosome reaction (AR). Finally, SNP affected a significant decrease in the rate of fertilization as well as blastocyst formation during early embryonic development. On the basis of these results, we propose that the effects of Ferritin on the AR may reduce overall sperm function leads to poor fertility in males and compromised embryonic development.

• 한국생물공학회:학술대회논문집
• /
• 한국생물공학회 2001년도 추계학술발표대회
• /
• pp.438-440
• /
• 2001

Ferritin an iron-storage protein. is found in bacteria and some animal tissues such as liver, spleen and bone marrow. It is more effective and causes less side reactions than traditional ferrous sulfate, which has been used primarily to treat iron deficiency in pregnancy anemia. Currently, the ferritin extracted from bovine and equine spleens are sold as a commercial product. Its markets are several hundreds of million US dollars. However, because of recent warnings against the viral diseases of animal origins such as mad cow disease, a safer ferritin is sought after. In this study, a production process for human ferritin was successfully developed. The amount of its produced in yeast is high enough to be economically viable.

• KSBB Journal
• /
• 제17권4호
• /
• pp.365-369
• /
• 2002

수용성 형태로 존재하는 융합 페리틴을 정제함에 있어서 실리카 분말을 이용한 전처리 공정은 전체 정제 공정효율 증가에 기여하였다. 전처리 공정을 통해 정제된 융합 페리틴의 순도를 높이기 위해 젤 여과 크로마토그래피를 통해 보다 정제된 응합 페리틴을 얻을 수 있었다. 이렇게 정제된 융합 페리틴의 철분결합능력을 분석해본결과 320 moles $F_{H}+F_{L}$ mole로 활성이 우수함을 알 수 있었으며, 분자량 분석을 통해 융합페리틴(40 k dalton)은 trimer와 monomer형태로 존재함을 확인할 수 있었다

• Journal of Nutrition and Health
• /
• 제54권5호
• /
• pp.435-447
• /
• 2021

Purpose: Body adiposity is negatively correlated with hepatic iron status, and Korean pine nut oil (PNO) has been reported to reduce adiposity. Therefore, we aimed to study the effects of PNO on adiposity, hepatic mineral status, and the expression of genes and proteins involved in iron absorption. Methods: Five-week-old male C57BL/6 mice were fed a control diet containing 10% kcal from PNO (PC) or soybean oil (SBO; SC), or a high-fat diet (HFD) containing 35% kcal from lard and 10% kcal from PNO (PHFD) or SBO (SHFD). Hepatic iron, copper, and zinc content; and expression of genes and proteins related to iron absorption were measured. Results: HFD-fed mice had a higher white fat mass (2-fold; p < 0.001), lower hepatic iron content (25% lower; p < 0.001), and lower hepatic Hamp (p = 0.028) and duodenal Dcytb mRNA levels (p = 0.037) compared to the control diet-fed mice. Hepatic iron status was negatively correlated with body weight (r = -0.607, p < 0.001) and white fat mass (r = -0.745, p < 0.001). Although the PHFD group gained less body weight (18% less; p < 0.05) and white fat mass (18% less; p < 0.05) than the SHFD group, the hepatic iron status impaired by the HFD feeding did not improve. The expression of hepatic and duodenal ferroportin protein was not affected by the fat amount or the oil type. PNO-fed mice had significantly lower Slc11a2 (p = 0.022) and Slc40a1 expression (p = 0.027) compared to SBO-fed mice. However, the PC group had a higher Heph expression than the SC group (p < 0.05). The hepatic copper and zinc content did not differ between the four diet groups, but hepatic copper content adjusted by body weight was significantly lower in the HFD-fed mice compared to the control diet-fed mice. Conclusion: HFD-induced obesity decreased hepatic iron storage by affecting the regulation of genes related to iron absorption; however, the 18% less white fat mass in the PHFD group was not enough to improve the iron status compared to the SHFD group. The hepatic copper and zinc status was not altered by the fat amount or the oil type.

• 한국축산식품학회지
• /
• 제32권2호
• /
• pp.162-167
• /
• 2012

Phosvitin was extracted from a chicken egg yolk and the iron-binding, along with antioxidative activity of the extracted phosvitin, was determined after mixing with ground beef at the concentrations of 100 and 500 mg/kg of meat. The electrophoretic pattern of the extracted phosvitin on SDS-PAGE was found to be identical to that of the standard phosvitin. The extracted phosvitin at $1,000{\mu}g$/mL showed an ability to bind approximately 65% of the iron in a 3 mM iron solution. Lipid oxidation was inhibited in the ground beef mixed with 500 mg/kg of the extracted phosvitin, during storage at $4^{\circ}C$ compared to that of the control (p<0.05). Additionally, color stability of ground beef containing the extracted phosvitin was enhanced (p<0.05). The pH, cooking loss, texture, and sensory properties of the ground beef were not affected, by adding up to 500 mg/kg of the extracted phosvitin. This result suggests that the phosvitin extracted from egg yolk could be used as an antioxidant reagent. In particular, phosvitin would be more amenable for use in meat products because it is a natural protein derived from animal products.

• 한국어병학회지
• /
• 제26권3호
• /
• pp.295-301
• /
• 2013

Ferritin is an evolutionarily conserved protein that plays an important role in iron storage and detoxification. In this study, the gene encoding a ferritin H subunit homologue (RbFH) was cloned from rock bream (Oplegnathus fasciatus) and analyzed at the expression. The full-length ferritin H cDNA was 1162 bp long and contained an open reading frame (ORF) of 531 bp that encoded 177 amino acid residues with a predicted molecular mass of 20.8 kDa. The 5' UTR was 297 bp in length, and the 3' UTR 298 bp, and preceded by a 5'-untranslated region that contains a putative Iron Regulatory Element (IRE). The deduced amino acid sequence of RbFH shares extensive sequence identities with the H ferritins of a number of fish species and contains the ferroxidase center that is preserved in ferritin H subunits. Examination of tissue specific expression indicated that RbFH expression was most abundant in PBLs, RBC, liver and muscle.

• Journal of Microbiology
• /
• 제44권1호
• /
• pp.54-63
• /
• 2006

Ferritin is a major eukaryotic protein and in humans is the protein of iron storage. A partial gene fragment of ferritin (255 bp) taken from the total RNA of Periserrula leucophryna, was amplified by RT-PCR using oligonucleotide primers designed from the conserved metal binding domain of eukaryotic ferritin and confirmed by DNA sequencing. Using the $^{32}P-labeled$ partial ferritin cDNA fragment, 28 different clones were obtained by the screening of the P. leucophryna cDNA library prepared in the Uni-ZAP XR vector, sequenced and characterized. The longest clone was named the PLF (Periserrula leucophryna ferritin) gene and the nucleotide and amino acid sequences of this novel gene were deposited in the GenBank databases with accession numbers DQ207752 and ABA55730, respectively. The entire cDNA of PLF clone was 1109 bp (CDS: 129-653), including a coding nucleotide sequence of 525 bp, a 5' -untranslated region of 128 bp, and a 3'-noncoding region of 456 bp. The 5'-UTR contains a putative iron responsive element (IRE) sequence. Ferritin has an open reading frame encoding a polypeptide of 174 amino acids including a hydrophobic signal peptide of 17 amino acids. The predicted molecular weights of the immature and mature ferritin were calculated to be 20.3 kDa and 18.2 kDa, respectively. The region encoding the mature ferritin was subcloned into the pT7-7 expression vector after PCR amplification using the designed primers and included the initiation and termination codons; the recombinant clones were expressed in E. coli BL21(DE3) or E. coli BL21(DE3)pLysE. SDS-PAGE and western blot analysis showed that a ferritin of approximately 18 kDa (mature form) was produced and that by iron staining in native PAGE, it is likely that the recombinant ferritin is correctly folded and assembled into a homopolymer composed of a single subunit.

• 생명과학회지
• /
• 제26권6호
• /
• pp.698-704
• /
• 2016

세포내소기관과 단백질 복합체의 운반은 kinesin superfamily proteins (KIFs)에 의해 매개된다. 처음으로 밝혀진 kinesin인 kinesin 1은 motor단백질로서 세포 내에서 미세소관을 따라 이동하며, 다양한 세포내 소기관이나 단백질복합체를 운반한다. Kinesin 1은 장쇄(KHC, 또한 KIF5s로도 통칭) 2분자와 단쇄(KLCs) 2분자로 구성된 4합체(tetramer) 구조를 가진다. KIF5s의 운반체 결합영역을 포함하는 말단영역은 다수의 운반체와 결합하지만, 결합운반체에 관하여 아직 충분히 밝혀지지 않았다. 본 연구에서 KIF5A의 결합 단백질을 동정하기 위하여 효모 two-hybrid screening을 수행하였고 철 저장 및 해독 기능을 하는 단백질인 ferritin heavy chain (Frt-h)을 찾아내었다. Frt-h은 KIF5A의 아미노산 800번과 940번 사이의 부위와 결합하며, 다른 KIF5s와도 결합함을 효모 two-hybrid assay로 확인하였다. 또한 Frt-h의 coiled-coil 도메인이 KIF5A와의 결합에 필수영역임을 밝혔다. 한편, ferritin light chain (Frt-l) 또한 KIF5s와 결합함을 효모 two-hybrid assay로 확인하였다. 이러한 단백질간의 결합을 glutathione S-transferase (GST) pull-down assay를 통하여 검증하였다. 추가적으로 생쥐의 뇌 파쇄액을 항 KHC 항체로 면역침강을 행한 결과, KLC1뿐만 아니라 Frt-h와 Frt-l도 같이 침강하였다. 이러한 결과들은 세포 내에서 kinesin 1이 ferritin 복합체를 운반함을 시사한다.