• Title/Summary/Keyword: double-labeling

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Localization of cytoskeletal proteins in Cryptosporidium parvum using double immunogold labeling (이중면역황금표지법을 이용한 작은와포자충의 세포골격 단백질 분포 관찰)

  • 유재란;이순형
    • Parasites, Hosts and Diseases
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    • v.34 no.4
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    • pp.215-224
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    • 1996
  • actin and some actin binding proteins such as tropomyosin, α-actinin and troponin T were localized by simultaneous double immunogold labeling in several developmental stages of Cryptosporidium parvum. All of the observed developmental stages have many paricles of tropomyosin and actin around pellicle and cytoplasm. Tropomyosin was labeled much more than the actin when these two proteins were labeled simultaneously. And α-actinin was labeled mostly in the pellicle, but troponin T labeling weas very rarely observed. From this study it was suggested that tropomyosin seemed to be one of the major proteins of C. parvum, so it must be playing important roles in C. parvum.

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DIFFERENCE CORDIALITY OF SOME SNAKE GRAPHS

  • Ponraj, R.;Narayanan, S. Sathish
    • Journal of applied mathematics & informatics
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    • v.32 no.3_4
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    • pp.377-387
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    • 2014
  • Let G be a (p, q) graph. Let f be a map from V (G) to {1, 2, ${\ldots}$, p}. For each edge uv, assign the label ${\mid}f(u)-f(\nu){\mid}$. f is called a difference cordial labeling if f is a one to one map and ${\mid}e_f(0)-e_f(1){\mid}{\leq}1$ where $e_f(1)$ and $e_f(0)$ denote the number of edges labeled with 1 and not labeled with 1 respectively. A graph with admits a difference cordial labeling is called a difference cordial graph. In this paper, we investigate the difference cordial labeling behavior of triangular snake, Quadrilateral snake, double triangular snake, double quadrilateral snake and alternate snakes.

Double Labeling of Binding Sites in Cellulosic Substrates Using Endo- and Exoglucanase-Gold Complexes

  • Bae Hyeun-Jong
    • Plant Resources
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    • v.8 no.3
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    • pp.175-180
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    • 2005
  • Thin sections of cellulose fibers were incubated with an endo- and an exoglucanase labeled with gold particles of differing sizes. The hydrolytic sites were then visualized under transmission electron microscopy (TEM). The potential interaction between the ${\beta}$-1, 4-glucan substrates and the endo- and the exoglucanases was investigated using cellulosic and lignocellulosic substrates. The simultaneous visualization was very successful in distinguishing preferred substrates for each cellulase in lignocellulosic substrates. When plant lignocellulose was preincubated with endocellulase, density of the gold labeling greatly increased suggesting that preliminary exposure of lignocellulosic material to endocellulase may have enhanced the accessibility of the substrate to endocellulase and exocellulase. This result provided a plausible explanation for the observed endo/exo cellulase co-hydrolysis.

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Determination of the Synthetic Time and the Transport Pattern of Vicilin and Legumin in Ginseng Endosperm Cell Using Double Immunogold Labeling (이중 면역금입자 표지법을 이용한 인삼 배유세포내 Vicilin과 Legumin의 합성시기 및 수송방식)

  • Lee, Chang-Seob;Yu, Seong-Cheol;Kim, Woo-Kap
    • Journal of Ginseng Research
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    • v.19 no.3
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    • pp.267-274
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    • 1995
  • Vicilin and legumin, the storage Proteins of seed, were Purified from ginseng (Panax ginseng C.A. Meyer) endosperm cells. They were immunized in rabbits, and antibodies were raised respectively. Using these two antibodies, double immunogold labeling of vicilin and legumin was carried out to determine the gap of synthetic time and the transport pattern of vicilin and legumin in the ginseng endosperm cells. Vicilin and legumin were synthesized at the same time at early embryo developmental stage. They were secreted from the Golgi bodies and accumulated into the small vacuoles. As the endosperm cells developed, vicilin and legumin localized in the small vacuoles were gradually transported toward the large central vacuole where they were stored. Protein bodies were derived from the vacuoles filled with proteins and distributed in the endosperm cells of mature red seed. Protein bodies were various in size from 1 to 8 ${\mu}{\textrm}{m}$ in which vicilin and legumin were mixed each other. The number of small particles labeled on the vicilin was greater than that of large particles labeled on the legumin in the protein bodies indicating that the amount of vicilin is higher than that of legumin in the protein bodies.

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Assignment of the Carbonyl Carbon Resonances in Anti-Dansyl Antibodies (항 단실 항체의 카르보닐탄소 유래 시그날의 귀속)

  • ;;Koichi Kato;Yoji Arata
    • YAKHAK HOEJI
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    • v.39 no.5
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    • pp.516-520
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    • 1995
  • The anti-dansyl antibodies were specifically labeled with stable isotope by growing hybridoma cells in serum-free medium. Assignments of the observed carbonyl carbon resonances have been determined by using $^{13}C-{15}N$ double labeling method in order to assign the Leu resonances. However, when the identical dipeptide appears more than twice in the polypeptide sequences, we applied the proteolytic fragments in the fragment-specific method. Carboxypep-tidase B-treated antibody has also been used to assign the Lys-447 in C terminal amino acid. These unambiguously assigned carbonyl carbon resonances in antibodies are thought to be useful in elucidating not only the structure of antibodies but also the structure-function relationship in the antibody by $^{13}C$ neuclear magnetic resonance spectroscopy.

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Expression of Kainate Glutamate Receptors in Type II Cells in Taste Buds of Rats

  • Lee, Sang-Bok;Lee, Cil-Han;Cho, Young-Kyung;Chung, Ki-Myung;Kim, Kyung-Nyun
    • International Journal of Oral Biology
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    • v.33 no.3
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    • pp.83-89
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    • 2008
  • Glutamate-induced cobalt uptake reveals non-NMDA glutamate receptors (GluRs) in rat taste bud cells. Previous studies suggest that glutamate-induced cobalt uptake in taste cells occurs mainly via kainate type GluRs. Cobaltstained cells were immunoreactive against GluR6 and KA1 subunits of GluRs. However, the functions of those type of receptors are not known yet. It is important question which types of taste cells are cobalt-stained when stimulated by glutamate and whether they express these kinds of GluRs. Circumvallate and foliate papilla of Sprague-Dawley rats (45-60 days old) were used. A cobalt-staining technique combined with immunohistochemistry against specific markers for taste bud cell types, such as blood group H antigen (BGH), $\alpha$-gustducin (Gus), or neural cell adhesion molecule (NCAM) was employed. We also performed double labeling of GluR6 or KA1 subunits of GluR with each specific marker for taste bud cell types. Lots of cobaltstained taste bud cells expressed Gus-like immunoreactivity, and subsets of the cobalt stained cells appeared NCAM- or BGH-like immunoreactivity. Stimulation with 1 mM glutamate significantly increased the number of cobaltstained cells in Gus-like immunoreactive cells, but not in NCAM- or BGH-like immunoreactive cells. In the double labeling experiments, GluR6 and KA1 subunits of GluRs were mainly expressed with Gus. These results suggest that kainate glutamate receptors preferentially expressed in type II taste bud cells in rat.

A double-labeling marker-based method for estimating inbreeding and parental genomic components in a population under conservation

  • Li, Wenting;Zhang, Mengmeng;Wang, Kejun;Lu, Yunfeng;Tang, Hui;Wu, Keliang
    • Asian-Australasian Journal of Animal Sciences
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    • v.33 no.1
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    • pp.12-23
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    • 2020
  • Objective: The objective of a conservation program is to maintain maximum genetic diversity and preserve the viability of a breed. However, the efficiency of a program is influenced by the ability to accurately measure and predict genetic diversity. Methods: To examine this question, we conducted a simulation in which common measures (i.e. heterozygosity) and novel measures (identity-by-descent probabilities and parental genomic components) were used to estimate genetic diversity within a conserved population using double-labeled single nucleotide polymorphism markers. Results: The results showed that the accuracy and sensitivity of identity-by-state probabilities and heterozygosity were close to identity by descent (IBD) probabilities, which reflect the true genetic diversity. Expected heterozygosity most closely aligned with IBD. All common measures suggested that practices used in the current Chinese pig conservation program result in a ~5% loss in genetic diversity every 10 generations. Parental genomic components were also analyzed to monitor real-time changes in genomic components for each male and female ancestor. The analysis showed that ~7.5% of male families and ~30% of female families were lost every 5 generations. After 50 generations of simulated conservation, 4 male families lost ~50% of their initial genomic components, and the genomic components for 24.8% of the female families were lost entirely. Conclusion: In summary, compared with the true genetic diversity value obtained using double-labeled markers, expected heterozygosity appears to be the optimal indicator. Parental genomic components analysis provides a more detailed picture of genetic diversity and can be used to guide conservation management practices.

Immunocytochemical Localization of Nitric Oxide Synthase-containing Neurons in Mouse and Rabbit Visual Cortex and Co-Localization with Calcium-binding Proteins

  • Lee, Jee-Eun;Jeon, Chang-Jin
    • Molecules and Cells
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    • v.19 no.3
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    • pp.408-417
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    • 2005
  • Nitric oxide (NO) occurs in various types of cells in the central nervous system. We studied the distribution and morphology of neuronal nitric oxide synthase (NOS)-containing neurons in the visual cortex of mouse and rabbit with antibody immunocytochemistry. We also compared this labeling to that of calbindin D28K, calretinin, and parvalbumin. Staining for NOS was seen both in the specific layers and in selective cell types. The densest concentration of intense anti-NOS immunoreactive (IR) neurons was found in layer VI, while the weak anti-NOS-IR neurons were found in layer II/III in both animals. The NOS-IR neurons varied in morphology. The large majority of NOS-IR neurons were round or oval cells with many dendrites coursing in all directions. Two-color immunofluorescence revealed that only 16.7% of the NOS-IR cells were double-labeled with calbindin D28K in the mouse visual cortex, while more than half (51.7%) of the NOS-IR cells were double-labeled with calretinin and 25.0% of the NOS-IR cells were double-labeled with parvalbumin in mouse. By contrast, 92.4% of the NOS-IR neurons expressed calbindin D28K while only 2.5% of the NOS-IR neurons expressed calretinin in the rabbit visual cortex. In contrast with the mouse, none of the NOS-IR cells in the rabbit visual cortex were double-labeled with parvalbumin. The results indicate that neurons in the visual cortex of both animals express NOS in specific layers and cell types, which do not correlate with the expression of calbindin D28K, calretinin or parvalbumin between the two animals.