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  • Immunocytochemistry  (856)
  • stability  (680)
  • Springer  (1,536)
  • 11
    Electronic Resource
    Electronic Resource
    Peptidergic motoneurons in the buccal ganglia of Aplysia californica Immunocytochemical, morphological, and physiological characterizations (1991)
    Springer
    Journal of comparative physiology 168 (1991), S. 323-336 
    Details
    ISSN: 1432-1351
    Keywords: Aplysia ; Motoneurons ; Immunocytochemistry ; Small cardioactive peptides ; Facilitation ; Depression ; Buccal ; Feeding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We used physiological recordings, intracellular dye injections and immunocytochemistry to further identify and characterize neurons in the buccal ganglia of Aplysia calif ornica expressing Small Cardioactive Peptide-like immunoreactivity (SCP-LI). Neurons were identified based upon soma size and position, input from premotor cells B4 and B5, axonal projections, muscle innervation patterns, and neuromuscular synaptic properties. SCP-LI was observed in several large ventral neurons including B6, B7, B9, B10, and B11, groups of s1 and s2 cluster cells, at least one cell located at a branch point of buccal nerve n2, and the previously characterized neurons B1, B2 and B15. B6, B7, B9, B10 and B11 are motoneurons to intrinsic muscles of the buccal mass, each displaying a unique innervation pattern and neuromuscular plasticity. Combined, these motoneurons innervate all major intrinsic buccal muscles (I1/I3, I2, I4, I5, I6). Correspondingly, SCP-LI processes were observed on all of these muscles. Innervation of multiple nonhomologous buccal muscles by individual motoneurons having extremely plastic neuromuscular synapses, represents a unique form of neuromuscular organization which is prevalent in this system. Our results show numerous SCPergic buccal motoneurons with widespread ganglionic processes and buccal muscle innervation, and support extensive use of SCPs in the control of feeding musculature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198352
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  • 12
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of reserve protein in the endoplasmic reticulum of developing bean (Phaseolus vulgaris) cotyledons (1980)
    Springer
    Planta 150 (1980), S. 419-425 
    Details
    ISSN: 1432-2048
    Keywords: Cotyledons ; Endoplasmic reticulum ; Ferritin labeling ; Immunocytochemistry ; Phaseolus ; Protein (reserve) ; Reserve protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ultrastructure of the storage parenchyma cells of the cotyledons of developing bean (Phaseolus vulgaris L.) seeds was examined in ultrathin frozen sections of specimens fixed in a mixture of glutaraldehyde, formaldehyde and acrolein, infused with 1 M sucrose, and sectioned at-80° C. Ultrastructural preservation was excellent and the various subcellular organelles could readily be identified in sections which had been stained with uranyl acetate and embedded in Carbowax and methylcellulose. The cells contained large protein bodies, numerous long endoplasmic reticulum cisternae, mitochondria, dictyosomes, and electron-dense vesicles ranging in size from 0.2 to 1.0 μm. Indirect immunolabelling using rabbit immunoglobulin G against purified phaseolin (7S reserve protein), and ferritin-conjugated goat immunoglobulin G against rabbit immunoglobulin G was used to localize phaseolin. With a concentration of 0.1 mg/ml of anti-phaseolin immunoglobin G, heavy labeling with ferritin particles was observed ober the protein bodies, the cisternae of the endoplasmic reticulum, and the vesicles. The same structures were lightly labeled when the concentration of the primary antigen was 0.02 mg/ml. Ferritin particles were also found over the Golgi bodies. The absence of ferritin particles from other organelles such as mitochondria and from areas of cytoplasm devoid of organelles indicated the specificity of the staining, especially at the lower concentration of anti-phaseolin immunoglobulin G.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00390179
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  • 13
    Electronic Resource
    Electronic Resource
    Subcellular localization of β-1,3-glucanase in Puccinia recondita f.sp. tritici-infected wheat leaves (1998)
    Springer
    Planta 204 (1998), S. 324-334 
    Details
    ISSN: 1432-2048
    Keywords: Key words:β-1 ; 3-Glucanase ; Immunocytochemistry ; Leaf rust pathogen ; Resistance ; Triticum (pathogen resistance)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. An antiserum raised against the purified 33-kDa β-1,3-glucanase of wheat (Triticum aestivum L.) was employed to investigate the ultrastructural localization of the enzyme in wheat leaves infected with Puccinia recondita Rob. ex Desm. f.sp. tritici Eriks. and Henn. using a post-embedding immunogold labelling technique. In both compatible and incompatible interactions, β-1,3-glucanase was detected in the host plasmalemma and in the domain of the host cell wall near the plasmalemma of the mesophyll cells, but higher concentrations of the enzyme were detected in infected resistant wheat leaves than in infected susceptible ones. β-1,3-Glucanase was also found in the secondary thickening of xylem vessels and in the walls of guard cells, epidermal cells and phloem elements, while no labelling was observed in host organelles, viz. vacuoles, mitochondria, endoplasmic reticulum, Golgi bodies, nuclei and chloroplasts. A low concentration of the enzyme was detected on the intercellular hyphal wall and in the hyphal cytoplasm. In the compatible interaction, β-1,3-glucanase was demonstrated to accumulate predominantly in the haustorial wall and extrahaustorial matrix. In the incompatible interaction, strong labelling for β-1,3-glucanase was found in host cell wall appositions, in the extracellular matrix in the intercellular space, and in electron-dense structures of host origin which occurred in the incompatible interaction only.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050263
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  • 14
    Electronic Resource
    Electronic Resource
    On the cellular localization of phosphoenolpyruvate carboxylase in Sorghum leaves (1981)
    Springer
    Planta 151 (1981), S. 226-231 
    Details
    ISSN: 1432-2048
    Keywords: Immunocytochemistry ; (PEP carboxylase) ; PEP carboxylase ; Sorghum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The localization of phosphoenol pyruvate carboxylase (EC 4.1.1.3.1.) in the leaf cells of Sorghum vulgare was investigated by using three techniques: the conventional aqueous and non aqueous methods gave conflicting results; the immunocytochemical techniques clearly showed that the enzyme is predominantly located in the cytoplasm of mesophyll cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395173
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  • 15
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of phaseolin and phytohemagglutinin in the endoplasmic reticulum and Golgi complex of developing bean cotyledons (1985)
    Springer
    Planta 164 (1985), S. 295-302 
    Details
    ISSN: 1432-2048
    Keywords: Cotyledon ; Golgi complex ; Immunocytochemistry ; Phaseolus (seed proteins) ; Phaseolin ; Phytohemagglutinin ; Protein (seeds)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Development of legume seeds is accompanied by the synthesis of storage proteins and lectins, and the deposition of these proteins in protein-storage vacuoles (protein bodies). We examined the subcellular distribution, in developing seeds of the common bean, Phaseolus vulgaris L., of the major storage protein (phaseolin) and the major lectin (phytohemagglutinin, PHA). The proteins were localized using an indirect immunocytochemical method in which ultrathin frozen sections were immunolabeled with rabbit antibodies specific for either PHA or phaseolin. Bound antibodies were then localized using goat-anti-rabbit immunoglobulin G adsorbed onto 4- to 5-nm colloidal gold particles. The sections were post-fixed with OsO4, dehydrated, and embedded in plastic on the grids. Both PHA and phaseolin exhibited a similar distribution in the storage-parenchyma cells, being found primarily in the developing protein bodies. Endoplasmic reticulum and Golgi complexes (cisternal stacks and associated vesicles) also were specifically labeled for both proteins, whereas the cytosol and other organelles, such as mitochondria, were not. We interpret these observations as supporting the hypothesis that the transport of storage proteins and lectins from their site of synthesis, the rough endoplasmic reticulum, to their site of deposition, the protein bodies, is mediated by the Golgi complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402940
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  • 16
    Electronic Resource
    Electronic Resource
    The major albumin protein from pea (Pisum sativum L.) (1985)
    Springer
    Planta 165 (1985), S. 522-526 
    Details
    ISSN: 1432-2048
    Keywords: Albumin (localisation) ; Cotyledon ; Pisum (albumin protein) ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The major albumin protein in storage parenchyma tissue of developing peas has been localised at an ultrastructural level by immunocytochemistry. Tissue was fixed in buffered aldehyde and embedded in LR White resin which was polymerised by addition of catalyst. Sections were labelled by the indirect method of absorption of Protein A-gold to specifically bound antibodies. This method gives high levels of specific labelling on sections which retain good ultrastructural preservation and have high contrast after conventional staining. The albumin is located throughout the cytoplasm although no labelling was found associated with the endoplasmic reticulum, Golgi apparatus, vacuoles-protein bodies or other organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00398098
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  • 17
    Electronic Resource
    Electronic Resource
    Immunochemical studies on xanthine dehydrogenase of soybean root nodules (1986)
    Springer
    Planta 167 (1986), S. 190-195 
    Details
    ISSN: 1432-2048
    Keywords: Glycine (xanthine dehydrogenase) ; Immunocytochemistry ; Polyclonal antibody ; Root nodule ; Xanthine dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Xanthine dehydrogenase (XDH, EC 1.2.1.37) was purified from root nodules of soybean (Glycine max) and used to prepare a polyclonal rabbit antiserum. Monospecificity of this antiserum was ascertained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the immunoprecipate. During root nodule development of soybean, only one form of XDH was detected on an immunological basis. Titration of XDH by immunoelectrophoresis showed that a remarkable increase in the amount of XDH occurred between two and four weeks after inoculation, in parallel with the increase in enzyme activity. Localization of XDH by immunofluorescence indicated that the enzyme was present exclusively in uninfected cells where it appeared to be associated with discrete organellels
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391414
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  • 18
    Electronic Resource
    Electronic Resource
    Opsin localization and chromophore retinoids identified within the basal brain of the lizard Anolis carolinensis (1993)
    Springer
    Journal of comparative physiology 172 (1993), S. 33-45 
    Details
    ISSN: 1432-1351
    Keywords: Photoreception ; Extraretinal Photoreceptor ; Chromophore ; Opsin ; Reptile ; Immunocytochemistry ; HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Since the beginning of this century evidence has accumulated which demonstrates that non-mammalian vertebrates possess photoreceptors situated deep within the brain. While many attempts have been made to localize these sensory cells, studies have either failed or been inconclusive. In this report we have used several experimental approaches to localize the deep brain photoreceptors of the lizard Anolis carolinensis. Using 3 antibodies that bind vertebrate cone opsins, we have immunolabelled cerebrospinal fluid (CSF)-contacting neurons located at the ventricular border within the nucleus ventromedialis of the septum. Western blot analysis indicates that these antibodies recognized a single 40 kD protein in ocular, anterior brain, and pineal extracts. Immunoblots of rodent brain did not show a similar protein band. We have also identified specific retinoids associated with phototransduction (11-cis and all-trans-3,4-didehydroretinaldehyde) within anterior brain extracts. This combined data provides the most detailed analysis of deep brain photoreceptors in any vertebrate. Consequently, we feel Anolis provides an excellent model to study this unexplored sensory system of the vertebrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214713
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  • 19
    Electronic Resource
    Electronic Resource
    Isolation of an egg-laying hormone-binding protein from the gonad of Aplysia californica and its localization in oocytes (1993)
    Springer
    Journal of comparative physiology 173 (1993), S. 475-483 
    Details
    ISSN: 1432-1351
    Keywords: Egg laying hormone ; Aplysia ; Binding protein ; Immunocytochemistry ; Reproductive system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A protein solubilized from a membrane preparation of the gonad of Aplysia californica has been isolated by affinity chromatography, using bag cell egg-laying hormone (ELH) as the bound ligand, and partially purified and characterized by gel electrophoresis. The protein has an apparent molecular weight of 52 kDa and consists of two disulfide-linked subunits of about 30 kDa each. The protein is glycosylated and has an acidic pI. Approximately 10–15 μg of this protein can be isolated from a single ovotestis, representing less than 1% of the total protein in the gonad; but the protein could not be detected in buccal mass or body wall, tissues which do not have apparent response to ELH. Antibodies generated against this ELH-binding protein (ELHBP) were used to localize sites in the ovotestis which might contain this molecule and thus represent targets for egg-laying hormone. Immunocytochemical results indicate that the oocytes are a rich source of this protein, since their cytoplasm was the only detectable site of immunoreactivity. Whether this binding protein represents an egg-laying hormone receptor is uncertain, but its prevalence in oocytes suggests that ELH plays a signaling role on these gametes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00193520
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  • 20
    Electronic Resource
    Electronic Resource
    A generalization of the Nash equilibrium theorem on bimatrix games (1996)
    Springer
    International journal of game theory 25 (1996), S. 1-12 
    Details
    ISSN: 1432-1270
    Keywords: Bimatrix game ; ɛ-equilibrium ; optimal strategies ; vertical linear complementarity problem ; degree ; stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics , Economics
    Notes: Abstract In this article, we consider a two-person game in which the first player picks a row representative matrixM from a nonempty set $$A$$ ofm ×n matrices and a probability distributionx on {1,2,...,m} while the second player picks a column representative matrixN from a nonempty set ℬ ofm ×n matrices and a probability distribution y on 1,2,...,n. This leads to the respective costs ofx t My andx t Ny for these players. We establish the existence of an ɛ-equilibrium for this game under the assumption that $$A$$ and ℬ are bounded. When the sets $$A$$ and ℬ are compact in ℝmxn, the result yields an equilibrium state at which stage no player can decrease his cost by unilaterally changing his row/column selection and probability distribution. The result, when further specialized to singleton sets, reduces to the famous theorem of Nash on bimatrix games.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01254380
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