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  • 1
    Electronic Resource
    Electronic Resource
    Linearity and hysteresis in the magnetoresistive response of (NiFe,NiFeCo)/Cu and Co/Cu/NiFe multilayers in patterned stripes : 38th Annual Conference on Magnetism and Magnetic Materials (1994)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 75 (1994), S. 6379-6381 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The linearity and hysteresis in the magnetoresistive (MR) response of NiFe/Cu and NiFeCo/Cu multilayers prepared by ion beam sputtering, and Cu/Co/Cu/NiFe multilayers prepared by MBE are investigated. These characteristics in the linear regions for the second peak of antiferromagnetically coupled NiFe/Cu multilayers are almost the same as those of NiFeCo/Cu ones at 50-Hz ac applied fields. The MR amplitude at the first peak is inferior to that at the second one, whereas, the linearity and hysteresis are superior. In weakly coupled Cu/Co/Cu/NiFe multilayers, a nonhysteretic MR response is obtained at a NiFe layer thickness of 10 A(ring). The linearity and symmetry around the zero magnetic field of the MR curve depend on the Cu layer thickness. When the thicknesses of the NiFe and Cu layers are 10 and 45 A(ring), respectively, good linearity and no hysteresis are observed without biasing techniques. The output levels in the linear regions of three different multilayers are 1.5–2.5 times as large as that of the conventional Permalloy film. These multilayers are promising materials for the fabrication of MR head for ultrahigh density recording.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.355356
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  • 2
    Electronic Resource
    Electronic Resource
    Linear magnetoresistive change at zero field in Cu/Co/Cu/NiFe multilayers (1993)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 63 (1993), S. 1702-1704 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Cu/Co/Cu/NiFe multilayers were prepared by molecular beam epitaxy and their magnetoresistive (MR) properties in dc and ac magnetic field were studied. With a view to application such as MR head, minor loops of MR transfer curves with applied fields of ±50 Oe were particularly investigated. By optimizing the thickness of each layer, a linear and nonhysteretic MR response was obtained. The output voltage was roughly estimated as two and a half times that of a conventional NiFe element in an ac magnetic field at 50 Hz.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.110690
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  • 3
    Electronic Resource
    Electronic Resource
    Resistivity vs. Magnetic structure in multilayers (1992)
    Springer
    Hyperfine interactions 68 (1992), S. 333-336 
    Details
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Mössbauer spectroscopy has been applied to study the interface magnetic propertics of multilayers exhibiting large magnetoresistance (MR) effects; Fe/Cr and Cu/Co/Cu/Fe. The temperature dependence of the local magnetization for the interface atom layers is found to be much smaller than that of the MR effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02396503
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  • 4
    Electronic Resource
    Electronic Resource
    Appearance of an intra-acrosomal antigen during the terminal step of spermiogenesis in the rat (1992)
    Springer
    Cell & tissue research 267 (1992), S. 203-208 
    Details
    ISSN: 1432-0878
    Keywords: Intra-acrosomal protein ; Monoclonal antibody ; Acrosome development ; Spermiogenesis ; Intracellular transport ; Testis ; Rat (Wistar) ; Mouse (ICR, BALB/c)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In a survey of sperm antigens in the rat, a new intra-acrosomal antigen was found using a monoclonal antibody MC41 raised against rat epididymal spermatozoa. The MC41 was immunoglobulin G1 and recognized spermatozoa from rat, mouse and hamster. Indirect immunofluorescence with MC41 specifically stained the crescent region of the anterior acrosome of the sperm head. Immuno-gold electron microscopy demonstrated that the antigen was localized within the acrosomal matrix. Immunoblot study showed that MC41 recognized a band of approximately 165000 dalton in the extract of rat sperm from the cauda epididymidis. Immunohistochemistry with MC41 demonstrated that the antigen was first detected in approximately step-2 spermatids, and distributed over the entire cytoplasmic region of spermatids from step 2 to early step 19. The head region became strongly stained in late step-19 spermatids and then in mature spermatozoa. Distinct immunostaining was not found in the developing acrosome of spermatids throughout spermiogenesis. These results suggest that the MC41 antigen is a unique intra-acrosomal antigen which is accumulated into the acrosome during the terminal step of spermiogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00302956
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  • 5
    Electronic Resource
    Electronic Resource
    Extra-Golgi pathway of an acrosomal antigen during spermiogenesis in the rat (1992)
    Springer
    Cell & tissue research 270 (1992), S. 451-457 
    Details
    ISSN: 1432-0878
    Keywords: Intra-acrosomal protein ; Acrosome development ; Extra-Golgi pathway ; Spermiogenesis ; Immunoelectron microscopy ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A monoclonal antibody (MC41) was produced that specifically recognizes a sperm acrosomal antigen of approximately 165000 dalton in the rat. Rat testis was examined using a pre-embedding immunoperoxidase technique to reveal the pathway of the MC41 antigen to the acrosome during spermiogenesis. The MC41 immunoreaction appeared in several organelles of spermatids in a stage-specific manner: (1) in the endoplasmic reticulum (ER) throughout spermiogenesis, (2) in the outer acrosomal membrane from steps 9 to 19, (3) as a weak immunoreaction in the vesicular structures in the acrosomal matrix from steps 11 to 17, and (4) as a strong immunoreaction in the acrosomal matrix especially at the terminal step of spermiogenesis (step 19). However, no immunoreaction was observed in the Golgi region throughout spermiogenesis. These results suggest that the pathway of the MC41 antigen leads firstly from the ER to the outer acrosomal membrane and secondly to the acrosomal matrix. This pathway does not involve the Golgi apparatus and is referred to as the “extra-Golgi pathway”.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00645046
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of the antigen recognized by a monoclonal antibody MN9: unique transport pathway to the equatorial segment of sperm head during spermiogenesis (1992)
    Springer
    Cell & tissue research 270 (1992), S. 459-468 
    Details
    ISSN: 1432-0878
    Keywords: Acrosome ; Equatorial segment of spermatozoa ; Transport pathway ; Spermiogenesis ; Monoclonal antibody ; Immuno-electron microscopy ; Mouse (BALB/c; CD-1; ICR) ; Rat (Wistar) ; Golden hamster-Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary MN9, a monoclonal antibody raised against mouse spermatozoa, specifically recognizes the equatorial segment of sperm head in several mammalian species, including humans. Colloidal gold-immuno-electron microscopy of mouse spermatozoa has shown that the antigen is localized in the space between the outer and inner acrosome membranes and on the acrosome membranes at the equatorial segment. Immunoblotting after electrophoresis of spermatozoa from the cauda epididymidis has identified two immunoreactive bands: 38 kDa and 48 kDa in mouse, and 48 kDa in rat. During spermiogenesis in rat, this antigen is transported to the equatorial segment via a unique pathway, first appearing in some cisternae of the endoplasmic reticulum and in the Golgi apparatus of spermatids at around step 3. The antigen can further be found on the vesicles at thetrans-side of the Golgi apparatus, in the matrix of the head cap, and on the head cap membrane in step-4 to step-7 spermatids. The antigen appears to be concentrated at the equatorial segment during late spermiogenesis. Neither the (pro-)acrosomic granule nor the surrounding membrane are required in this pathway. This pathway can be termed the ‘Golgi-head cap tract’.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00645047
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  • 7
    Electronic Resource
    Electronic Resource
    Intra-acrosomal organization of a 90-kilodalton antigen during spermiogenesis in the rat (1994)
    Springer
    Cell & tissue research 277 (1994), S. 61-67 
    Details
    ISSN: 1432-0878
    Keywords: Acrosome development ; Antigen localization ; Intra-acrosomal migration ; Golgi apparatus ; Spermiogenesis ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The localization of an acrosomal protein was studied using a monoclonal antibody MN7 raised against mouse spermatozoa. MN7 specifically recognized the anterior acrosome of several mammalian (mouse, rat, hamster) spermatozoa fixed with paraformaldehyde. An immunoblot study with periodate treatment showed that MN7 recognized a carbohydrate region of a 90 kDa protein in an extract of mouse and rat cauda epididymal spermatozoa. The change in distribution of the MN7 antigen during acrosome development was investigated in the rat testis using the pre-embedding immunoperoxidase technique. The antigen first appeared in the proacrosomic granules of spermatids in steps 1–2. Small vesicles adjacent to the outer acrosomal membrane and the developing acrosomic system were immunoreactive during steps 4–7. The majority of the antigen was then redistributed to the head-cap portion during steps 8–18, and finally restricted to the anterior acrosome in the step 19-spermatid. These results suggest that the antigen is transported to the acrosome by way of the vesicles that originate from the Golgi apparatus during early spermiogenesis, and are then delivered to the final destination within the acrosome by the intra-acrosomal migration during late spermiogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303081
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  • 8
    Electronic Resource
    Electronic Resource
    Intra-acrosomal organization of a 90-kilodalton antigen during spermiogenesis in the rat (1994)
    Springer
    Cell & tissue research 277 (1994), S. 61-67 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Acrosome development – Antigen localization – Intra-acrosomal migration – Golgi apparatus – Spermiogenesis – Immunocytochemistry – Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The localization of an acrosomal protein was studied using a monoclonal antibody MN7 raised against mouse spermatozoa. MN7 specifically recognized the anterior acrosome of several mammalian (mouse, rat, hamster) spermatozoa fixed with paraformaldehyde. An immunoblot study with periodate treatment showed that MN7 recognized a carbohydrate region of a 90 kDa protein in an extract of mouse and rat cauda epididymal spermatozoa. The change in distribution of the MN7 antigen during acrosome development was investigated in the rat testis using the pre-embedding immunoperoxidase technique. The antigen first appeared in the proacrosomic granules of spermatids in steps 1–2. Small vesicles adjacent to the outer acrosomal membrane and the developing acrosomic system were immunoreactive during steps 4–7. The majority of the antigen was then redistributed to the head-cap portion during steps 8–18, and finally restricted to the anterior acrosome in the step 19-spermatid. These results suggest that the antigen is transported to the acrosome by way of the vesicles that originate from the Golgi apparatus during early spermiogenesis, and are then delivered to the final destination within the acrosome by the intra-acrosomal migration during late spermiogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303081
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  • 9
    Electronic Resource
    Electronic Resource
    S8.25 A new family of C-P glycosphingolipids in aplysia: Structures and functions (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 273-273 
    Details
    ISSN: 1573-4986
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01209967
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  • 10
    Electronic Resource
    Electronic Resource
    A rat sperm flagellar surface antigen that originates in the testis and is expressed on the flagellar surface during epididymal transit (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 32 (1992), S. 399-408 
    Details
    ISSN: 1040-452X
    Keywords: Monoclonal antibody ; MC31 ; Spermatogenesis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We identified a rat sperm flagellar surface antigen using an IgG1 monoclonal antibody (MC31) against rat epididymal sperm. Avidin-biotin-peroxidase immunohistochemistry demonstrated that the antigen was first expressed in the cytoplasm of early primary spermatocytes, then gradually became restricted to the principal piece of the sperm flagellum during spermatogenesis. However, when the sperm reached the corpus epididymidis, the antigen was expressed on the surface of both the principal piece and the midpiece of the flagellum. The epithelial cells of the epididymis were not stained with MC31. Immunogold electron microscopy showed that the antigen was present on the surface of the sperm flagellar plasma membrane. Immunoblotting of Triton X-100 extracts of epididymal sperm after one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions demonstrated that MC31 detected a major antigen of 26,000-28,000 daltons (26-28K). Two-dimensional isoelectric focusing and SDS-PAGE indicated that the 26-28K antigen had an isoelectric focusing point (pl) of 5.8-5.3; minor antigens were also detected from 26K (pl 5.8) to 35K (pl 5.0). These results indicate that the antigen recognized by MC31 is an acidic 26-35K protein that originates in the testis, is integrated into the sperm flagellar plasma membrane of the principal piece during spermatogenesis, and then is expressed on the entire flagellar surface during epididymal transit. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080320415
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