• Title/Summary/Keyword: colloidal gold

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Immunoelectron Microscopic Localization and Analysis of Herpes simplex Virus Type 2 Antigens (전자현미경 기법을 이용한 Herpes simplex 2형 바이러스 항원의 면역학적 분석)

  • 김천식;오명환
    • Korean Journal of Microbiology
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    • v.40 no.1
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    • pp.23-28
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    • 2004
  • Antigenic analysis of Herpes simplex type 2 virus was performed and its major antigen was localized using an immunoelectron microscopy. Antigens of 32, 43, 59 and 69 kDa were constantly expressed during the course of infection for 48 hr in the infected Vero cell. An antigen of 51 kDa was turned out to be the major one in inducing a immune response in Western-blot analysis. The 51 kDa antigen was localized on the surface of HSV-2 by immunoelectron microscopy using colloidal golds and anti-HSV 2 polyc1onal antibody. Immunofluorescence assay indicated that viral antigens were found throughout the infected cell and, especially, on the surface of the cell.

Immunocytochemical Localization of Vicilin in Endosperm Cells of Panax ginseng C.A. Meyer (인삼(Panax ginseng C.A. Meyer) 배유세포내 Vicilin의 면역세포화학적 분포)

  • 이창섭
    • Journal of Plant Biology
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    • v.35 no.2
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    • pp.99-106
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    • 1992
  • The endosperm protein, vicilin, of ginseng (Panax ginseng C.A. Meyer) was purified by ammonium sulfate precipitaion, gel permeation and ion exchange column chromatography. Vicilin is a glycoprotein composed of 2 subunits with molecular masses of 55,000 (large subunit) and 44,000 (small subunit). The anti-vicilin antibody was raised in rabbit, and purified by DEAE Affi-Gel Blue affinity chromatography. The endosperm cells of the seed were reacted with this anti-vicilin antibody and colloidal gold conjugated secondary antibody. Gold particles were labelled on the elaborating granules of Golgi complex, electron-dense granules and protein bodies in the endosperm cells. These results indicated that the vicilin, which was synthesized in rough endoplasmic reticulum and transported to Golgi, was elaborated in saccules of the Golgi and then transported into protein bodies by electron-dense granules.anules.

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An Immunocytochemical Study on Storage Proteins of Ginseng Seed - Tris Buffer Soluble Protein - (인삼 종자의 저장단백질에 관한 면역 세포화학적 연구 - Tris 완충액 가용성 단백질 -)

  • Kim, Woo-Kap
    • 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.

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Evaluation of Rapid IgG4 Test for Diagnosis of Gnathostomiasis

  • Wang, Yue;Ma, An;Liu, Xiao-Long;Eamsobhana, Praphathip;Gan, Xiao-Xian
    • Parasites, Hosts and Diseases
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    • v.59 no.3
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    • pp.257-263
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    • 2021
  • Human gnathostomiasis is a parasitic disease caused by Gnathostoma nematode infection. A rapid, reliable, and practical immunoassay, named dot immuno-gold filtration assay (DIGFA), was developed to supporting clinical diagnosis of gnathostomiasis. The practical tool detected anti-Gnathostoma-specific IgG4 in human serum using crude extract of third-stage larvae as antigen. The result of the test was shown by anti-human IgG4 monoclonal antibody conjugated colloidal gold. The sensitivity and specificity of the test were both 100% for detection in human sera from patients with gnathostomiasis (13/13) and from healthy negative controls (50/50), respectively. Cross-reactivity with heterogonous serum samples from patients with other helminthiases ranged from 0 (trichinosis, paragonimiasis, clonorchiasis, schistosomiasis, and cysticercosis) to 25.0% (sparganosis), with an average of 6.3% (7/112). Moreover, specific IgG4 antibodies diminished at 6 months after treatment. This study showed that DIGFA for the detection of specific IgG4 in human sera could be a promising tool for the diagnosis of gnathostomiasis and useful for evaluating therapeutic effects.

Latent fingerprint development from rubber gloves using MMD I (Multimetal deposition I)

  • An, Jaeyoung;Kim, Heesu;Oh, Jungmin;Han, Sooyong;Yu, Jeseol
    • Analytical Science and Technology
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    • v.33 no.2
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    • pp.108-114
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    • 2020
  • Gloves are very important evidence at a crime scene; specifically, rubber gloves can be found easily at homes. Therefore, crime scene investigators attempt to develop fingerprints inside the rubber gloves that are discovered, for identifying unknown suspects. This study compared the effectiveness of three different methods that are used for developing latent prints on gloves with aging time. These were the powder, cyanoacrylate fuming, and multi-metal deposition I methods. The powder method achieved good results for 1-3 days of aged prints, and the cyanoacrylate fuming method worked well on 2-week-old prints. In comparison, multi-metal deposition I method developed good quality fingerprints for 6 weeks of aging time.

Contact Transfer Printing Using Bi-layer Functionalized Nanobio Interface for Flexible Plasmonic Sensing

  • Lee, Jihye;Park, Jiyun;Lee, Junyoung;Yeo, Jong-Souk
    • Proceedings of the Korean Vacuum Society Conference
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    • 2014.02a
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    • pp.413-413
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    • 2014
  • In this paper, we present a fabrication method of functionalized gold nanostructures on flexible substrate that can be implemented for plasmonic sensing application. For biomolecular sensing, many researchers exploit unconventional lithography method like nanoimprint lithography (NIP), contact transfer lithography, soft lithography, colloidal transfer printing due to its usability and easy to functionalization. In particular, nanoimprint and contact transfer lithography need to have anti-adhesion layer for distinctive metallic properties on the flexible substrates. However, when metallic thin film was deposited on the anti-adhesion layer coated substrates, we discover much aggravation of the mold by repetitive use. Thus it would be impossible to get a high quality of metal nanostructure on the transferred substrate for developing flexible electronics based transfer printing. Here we demonstrate a method for nano-pillar mold and transfer the controllable nanoparticle array on the flexible substrates without an anti-adhesion layer. Also functionalization of gold was investigated by the different length of thiol applied for effectively localized surface plasmonic resonance sensing. First, a focused ion beam (FIB) and ICP-RIE are used to fabricate the nanoscale pillar array. Then gold metal layer is deposited onto the patterned nanostructure. The metallic 130 nm and 250 nm nanodisk pattern are transferred onto flexible polymer substrate by bi-layer functionalized contact imprinting which can be tunable surface energy interfaces. Different thiol reagents such as Thioglycolic acid (98%), 3-Mercaptopropionic acid (99%), 11-Mercaptoundecanoic acid (95%) and 16-Mercaptohexadecanoic acid (90%) are used. Overcoming the repeatedly usage of the anti-adhesion layer mold which has less uniformity and not washable interface, contact printing method using bi-layer gold array are not only expedient access to fabrication but also have distinctive properties including anti-adhesion layer free, functionalized bottom of the gold nano disk, repeatedly replicate the pattern on the flexible substrate. As a result we demonstrate the feasibility of flexible plasmonic sensing interface and anticipate that the method can be extended to variable application including the portable bio sensor via mass production of stable nanostructure array and other nanophotonic application.

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The Effect of Acute Sinusitis on the Ultrastructure and Sialic Acid Distribution on the Sinus Mucosa Cell Surface of the Rabbit (실험토끼 상악동염이 상피세포 표면의 미세구조변화와 Sialic acid의 분포에 미치는 영향)

  • Kim, Soo-Jin;Lee, Eun-Jung
    • Applied Microscopy
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    • v.32 no.2
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    • pp.163-170
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    • 2002
  • Experimatal maxillary sinusitis was induced in New Zealand white rabbits by blocking the maxillary sinus ostium. The distribution of lectin receptors was explored in the mucosa with induced maxillary sinusitis using colloidal gold label complex with lectin WGA purified from wheat germ (Triticum vulgaris). The lectin WGA gold complex, shown to recognize GlcNac (N-acetylglucosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections and viewed under the electron microscope. An increased height of the cylindric cells, ciliary loss and hyperplasia of the secretory cells were observed. Examination of normal sinus mucosa labeled with gold-labeled lectins showed the distribution of sialoglycoconjugates to be mainly in the ciliary layer and the granules in the secretory cells. Inflamed mucosa had increased labeling intensity of gold-labeled WGA in the cilia and the secretory granules. These results indicate that lectin WGA receptors are located in the cilia and secretory granules. Specific changes in the lectin binding pattern were apparent in the inflamed mucosa in the experimentally induced acute sinusitis, in comparison with normal mucosa, conceivably as a part of host defense reactions.

Ultrastructural Change of the Bile Duct Fibroblast at Infected Rat with Clonorchis sinensis (간흡충에 감염된 실험쥐 담관 섬유모세포의 미세구조적 변화)

  • Kim, Soo-Jin;Min, Byoung-Hoon
    • Applied Microscopy
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    • v.34 no.2
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    • pp.121-130
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    • 2004
  • In this study, ultrastructural change of the bile duct fibroblast at infected rat with Clonorchis sinensis, and the distribution of lectin receptors and actin protein in cultured bile duct infected with Clonorchis sinensis. It explored using colloidal gold label complex with lectin WGA purified from wheat germ (Triticum vulgaris) and anti actin antibody purified actin (43 kDa) isolated from chicken back muscle. The lectin WGA with protein A gold complex labeled sections of the cultured fibroblast revealed gold particles specifically distributed on the multi vesicular form Golgi complex and cell surface of the fibroblast. The actin antibody with protein A gold complex labeled sections of the cultured fibroblast revealed gold particles specifically distributed on the cytoplasm of the fibroblast. Labeling of cultured fibroblast in rat bile duct infected with Clonorchis sinensis was then quantified and compared to that of cultured Fibroblast in Rat Bile duct. These results indicate that lectin WGA receptors are located in the multi vesicular form Golgi complex in the cytoplasm to the cytoplasmic process of the Rat bile duct fibroblast infected with Clonorchis sinensis. Therefore, the GlcNAc and NeuNac regions on the cell surface and cytoplasmic process appear to be functionally associated with cell-recognition and protection from other cell of the tissue, and linked with secretion and exocytosis of the fibroblst cytoplasm. GlcNAc and NeuNAc product in the multi vesicular form Golgi complex then it is transported to cell surface. Actin protein is many appears that infected fibroblast rather than normal fibroblast. The fibroblast of infected with Clonorchis sinensis are against of the physical and chemical stimulation. Then development of cytoplasmic process is relative some stimulation.

Hepatosplenic Scanning with $^{198}Au$ Colloidal Gold in Chronic Myelogenous Leukemia (만성골수성백혈병(慢性骨髓性白血病)에 있어서 $^{198}Au$교질(膠質)을 사용(使用)한 간비주사소견(肝脾走査所見))

  • Lee, Kyu-Bo
    • The Korean Journal of Nuclear Medicine
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    • v.13 no.1_2
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    • pp.15-21
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    • 1979
  • From January 1975 to March 1978, 18 cases of chronic myelogenous leukemia diagnosed at Kyungpook National University Hospital were tested by hepatosplenic scanning with $^{198}Au$ colloidal gold. The photo scanning findings in relation to clinical and laboratory findings are following. 1) Male to female ratio was 2:1 and 2nd and 3rd decades were predominant. 2) No focal space-occupying lesion was noticed both in the liver and spleen. 3) 4 cases revealed well visualization of spleen, 7 cases poor visualization, and 7 cases nonvisualization. 4) No significant difference between well visualization group and poor visualization group was noted in clinical findings, liver function test and hematologic findings. 5) Cases with nonvisualization of the spleen tended to be associated with thrombocytopenia, decreased megakaryocytes in the marrow and longer duration of the illness.

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Fine Structural Characterization and Localization of Lectin Receptors in the Cultured Fibroblast (배양 섬유 세포에 있어서 세포 표면의 미세구조적 특성과 당단백 (lectin WGA 수용체)의 분포)

  • Kim, Soo-Jin;Hahm, So-Young
    • Applied Microscopy
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    • v.31 no.1
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    • pp.49-57
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    • 2001
  • In this study, the distribution of lectin receptors in culutured fibroblast was explored using colloidal gold label complexed with lectin WGA purified from wheat germ (Triticum vulgare). The lectin WGA gold complex, shown to recognize GlcNAc (N-acetylgalactosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections viewed under electron microscope Labeled sections of the culutured fibroblast revealed gold particles specifically distributed on the cytoplasm and cell surface of the fibroblast. Labeling of 24 hours culutured fibroblast was then quantified and compared to that of 72 hours culutured fibroblast. 24 hours culutured fibroblast sections resulted in specific gold particle distribution on the cytoplasmic vesicle of the culutured fibroblast. These results indicate that lectin WGA receptors are located in the cytoplasmic vesicle and cell surface of the 24 hours culutured fibroblast, and on the cell surface of the 72 hours culutured fibroblast. Therefore, the GlcNAc and NeuNAc regions on the cell surface appear to be functionally associated with cell-recognition and protection from other cell of the tissue, and linked with secretion and exocytosis of the fibroblast cytoplasm.

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