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  • 1985-1989  (19)
  • 1
    Electronic Resource
    Electronic Resource
    Diamond films for laser hardening (1989)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 54 (1989), S. 2728-2730 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Diamond has many unique physical properties useful as thin-film coatings for laser optics. The calculated value of the laser-induced stress resistance parameter of diamond is orders of magnitude higher than any other material and, therefore, diamond films should have a higher laser damage threshold. This is confirmed by laser damage experiments carried out on free-standing polycrystalline diamond films. Materials susceptible to laser damage can be protected by diamond thin-film coatings to enhance the damage threshold. This is demonstrated in the case of diamond coated silicon substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.101004
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  • 2
    Electronic Resource
    Electronic Resource
    On epitaxial growth of diamond films on (100) silicon substrates (1988)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 53 (1988), S. 1823-1825 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We have investigated characteristics of polycrystalline diamond thin films formed by plasma-enhanced chemical vapor deposition method on silicon substrates using Raman spectroscopy, analytical and high-resolution transmission electron microscopy techniques. Grains with average size 1 μm in diameter were observed in these films. The Raman spectra from these films contain the strongest peak at 1335 cm−1, providing the characteristic signature for sp3 (diamond) bonding. The broad peak centered around 1550 cm−1 is believed to be due to some graphitic bonding. From detailed high-resolution images and microdiffraction, films were characterized to be cubic diamond with a lattice parameter of 3.56 A(ring). Diamond crystallites with fivefold external morphologies were also observed. The large crystallites in the films exhibited preferential texture in 〈011〉 type orientations. These crystallites were found to be twinned in {111} planes. The large 〈011〉 crystallites exhibited matching in {111} or {200} lattice planes of diamond with {022} planes of silicon. This is in agreement with our previous work on the growth of Ni on MgO, which showed that textured growth can occur by matching a set of lattice planes in the absence of matching of lattice constants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.99791
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  • 3
    Electronic Resource
    Electronic Resource
    Neurotransmitter Modulation of the Human Class II Gene DRα on Multiforme Glioblastoma Cell Lines A Molecular Analysis (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 540 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb27141.x
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  • 4
    Electronic Resource
    Electronic Resource
    Acute nonlymphocytic leukemia (M2) with chromosome abnormality trisomy 4 developing eight years after radiation therapy for breast cancer (1989)
    Springer
    Annals of hematology 58 (1989), S. 27-31 
    Details
    ISSN: 1432-0584
    Keywords: Chromosome ; ANLL ; Trisomy 4 ; L-CFU ; CFU mix
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We report here the development, 8 years after radiation therapy for breast cancer, of acute nonlymphocytic leukemia (ANLL), type M2 of the FAB classification, in which trisomy 4 was detected as the only chromosomal abnormality. Simultaneous observation of cytologic and cytogenetic features of individual colonies derived from leukemic progenitor (L-CFU) and early progenitor (CFU mix) cultures in this patient revealed that all colonies examined had a normal karyotype, although the clone with trisomy 4 was predominant in the direct bone-marrow culture. These findings suggest that progenitor cells with trisomy 4 were less predominant in colony growth when stimulated by colony-stimulating factors (CSFs) than were stem cells with a normal karyotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00320232
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  • 5
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of cathepsin H in rat kidney (1986)
    Springer
    Histochemistry and cell biology 85 (1986), S. 223-230 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Light and electron microscopic localization of cathepsin H in rat kidney was studied using post-embedding immunocytochemical techniques. For ligh microscopy, Epon sections of the kidney were stained by immunoenzyme method after removal of Epon and for electron microscopy, ultrathin sections of the Lowicryl K4M-embedded material were labeled by protein A-gold (pAg) technique. By light microscopy, fine granular staining was found in throughout the nephron, but the staining intensity considerably varied. The strongest staining was noted in the S1 segment of the proximal tubules followed by the S2 and S3 segments and the medullary collecting tubules. The glomeruli, the distal tubules, and the cortical collecting tubules were weakly stained. By electron microscopy, a gold label was found exclusively in lysosomes, which showed various sizes and labeling intensity. The results were quite consistent with the light microscopic results. The labeling intensity tended to increase as the matrix of lysosomes was condensed. Quantitative analysis of the labeling density of lysosomes demonstrated that the highest labeling density is found in the S1 segment of the proximal tubules and the labeling density of other renal segments is significantly low levels. The results indicate that a main site for cathepsin H in rat kidney is the S1 segment of the proximal tubules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00494808
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  • 6
    Electronic Resource
    Electronic Resource
    Immunocytochemical demonstration of serine:pyruvate aminotransferase in peroxisomes and mitochondria of rat kidney (1985)
    Springer
    Histochemistry and cell biology 83 (1985), S. 81-85 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The light- and electron-microscopic localization of serine:pyruvate aminotransferase (SPT) in rat kidney was studied using immunoenzyme and protein A-gold techniques. Rat kidneys were fixed by perfusion through the abdominal aorta and small tissue slices were embedded in Epon, Lowicryl K4M, or LR Gold. The Epon was removed from the semithin sections, which were then stained using the immunoenzyme technique. Ultrathin sections of Lowicryl K4M- or LR gold-embedded materials were labeled using the protein A-gold technique. At light microscopy, discrete granular reaction deposits were exclusively present in the proximal tubule, all of whose segments were positive for SPT. A weakly positive reaction was observed in the distal tubules. At electron microscopy, gold particles indicating the antigenic sites for SPT were confined to the peroxisomes and mitochondria. The labeling intensity of both organelles was dependent on the embedding resins used. The labeling of Lowicryl K4M-embedded material was weaker than that of LR gold-embedded material; Quantitative analysis confirmed this result. Our results indicate that, in rat kidney, the main intracellular sites for SPT are peroxisomes and mitochondria of the proximal tubule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495305
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  • 7
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of cathepsins B and H in rat liver (1987)
    Springer
    Histochemistry and cell biology 88 (1987), S. 97-103 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Light and electron microscopic localization of cathepsins B and H in rat liver was investigated by immunoenzyme and protein A-gold techniques. For light microscopy (LM), semi-thin sections of the Epon-embedded material were stained by the immunoenzyme technique after removal of epoxy resin. For electron microscopy (EM), ultrathin sections of the Lowicryl K4M-embedded material were stained by the protein A-gold technique. By LM, reaction deposits for cathepsins B and H were present in the cytoplasmic granules of parenchymal cells and endothelial cells, and Kupffer cells. The sinus-lining cells and the parenchymal cells showed the similar staining intensity. By EM, gold particles were present exclusively in lysosomes of all the cell types cited above. The same results were obtained from quantitative analysis. In addition, Golgi complexes themselves were mostly negative but some small vesicles on the trans side of them were labeled for these proteinases. The results indicate that cathepsins B and H are present in the lysosomes of rat liver and that these enzymes seem to be transported by small vesicles from endoplasmic reticulum to lysosomes via tubuloreticular network of the trans Golgi region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490174
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  • 8
    Electronic Resource
    Electronic Resource
    Localization of cathepsin L in rat kidney revealed by immunoenzyme and immunogold techniques (1988)
    Springer
    Histochemistry and cell biology 90 (1988), S. 277-283 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Localization of cathepsin L in rat kidney was investigated by immunocytochemical techniques. Kidneys were fixed by perfusion and embedded in Epon or Lowicryl K4M without postomication. For light microscopy (LM), semi-thin sections of the Epon-embedded material were stained by the immunoenzyme technique after removal of epoxy resin. For electron microscopy (EM), ultra-thin sections of Lowicryl K4M-embedded material were stained by the protein A-gold technique. By LM, reaction deposits for cathepsin L were present in the cytoplasmic granules of proximal tubule cells, but little or no reaction product was noted in distal tubule, collecting tubule, and most of urinary tubules in the medulla. By EM, heavy gold label for cathepsin L was confined exclusively to lysosomes of the proximal tubule cells, but little or no label to those of the other segments. In immunocytochemical control sections, no reaction was observed. These results indicate that a main container of cathepsin L is lysosomes of the proximal tubule and suggest that the enzyme plays a role in the degradation of endocytosed proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495971
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  • 9
    Electronic Resource
    Electronic Resource
    Light and electron microscopic localization of l-alpha-hydroxyacid oxidase in rat kidney revealed by immunocytochemical techniques (1985)
    Springer
    Histochemistry and cell biology 82 (1985), S. 25-32 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Light and electron microscopic localization of l-alpha-hydroxyacid oxidase (l-HOX) in rat kidney was studied by means of immunocytochemical · techniques. Isozymes A and B of l-HOX were purified from rat liver and kidney, respectively. The apparent molecular weights of the subunits of the isozymes A and B were 35,800 and 33,500 daltons, respectively, by a slab gel electrophoresis. Antibodies to the isozymes were raised in rabbits. Anti(isozyme A) is not cross-reactive with the isozyme B and vice versa anti(isozyme B) not with the isozyme A. Using anti-isozyme B, semithin sections of Epon-embedded material and ultrathin sections of Lowicryl K4M-embedded material were stained by immunoenzyme and protein A-gold techniques, respectively. By light microscopy, fine discrete granular staining was noted in proximal tubules, but not in distal tubules including thick and thin limbs of Henle and collecting tubules. By electron microscopy, gold particles representing the antigen sites for l-HOX B were confined exclusively to peroxisomes, in which most of the gold particles were localized in electron dense peripheral matrix, but little in central matrix with low electron density. The results indicate that l-HOX B does not homogeneously distribute in peroxisomes of rat kidney but might be associated with some substructure within peroxisome matrix.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00502087
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  • 10
    Electronic Resource
    Electronic Resource
    Localization of cathepsin D in rat liver (1985)
    Springer
    Histochemistry and cell biology 82 (1985), S. 141-148 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Light and electron microscopic localization of cathepsin D in rat liver was investigated by post-embedding immunoenzyme and protein A-gold techniques. By light microscopy, cytoplasmic granules of parenchymal cells and Kupffer cells were stained for cathepsin D. Weak staining was also noted in sinusoidal endothelial cells. In the parenchymal cells many of positive granules located around bile canaliculi. In the Kupffer cells and the endothelial cells, diffuse staining was noted in the cytoplasm in addition to granular staining. By electron microscopy, gold particles representing the antigenic sites for cathepsin D were seen in typical secondary lysosomes and some multivesicular bodies of the parenchymal cells and Kupffer cells. The lysosomes of the endothelial cells and fat-storing cells were weakly labeled. Quantitative analysis of the labeling density in the lysosomes of these three types of cells demonstrated that the lysosomes of parenchymal cells and Kupffer cells are main containers of cathepsin D in rat liver. The results suggest that cathepsin D functions in the intracellular digestive system of parenchymal cells and Kupffer cells but not so much in that of the endothelial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00708198
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