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1

Digitale Medien

Monoclonal antibodies which recognize different cell types in the rat retina (1980)

Barnstable, Colin J.

[s.l.] : Nature Publishing Group

Nature 286 (1980), S. 231-235

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ISSN: 1476-4687

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Notizen: [Auszug] Seven monoclonal antibodies have been produced against a membrane preparation from adult rat retina. Three antibodies reacted with particular regions of rat photoreceptor cell surfaces: RET-P1 labelled the cell bodies, outer and inner segments (rods but not cones), RET-P2 labelled only outer ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/286231a0

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2

Digitale Medien

Molecular heterogeneity and the nervous system (1982)

Barnstable, Colin J.

[s.l.] : Nature Publishing Group

Nature 298 (1982), S. 708-709

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ISSN: 1476-4687

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Notizen: [Auszug] THE nervous system has an anatomical and physiological complexity that is considerably greater than that of other tissues and is seemingly part of a generally increased level of molecular complexity. The complexity arises both because the nervous system consists of more cell types and subtypes than ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/298708a0

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3

Digitale Medien

A gradient of membrane protein in the retina (1981)

Barnstable, Colin J.

[s.l.] : Nature Publishing Group

Nature 292 (1981), S. 13-14

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ISSN: 1476-4687

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Notizen: [Auszug] THE MECHANISM by which cells sense and signal their position within an organ or organism remains one of the least understood problems in biology. Many experimental systems such as chick limb development, hydra regeneration and insect cuticle formation have indicated that gradients of positional ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/292013a0

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4

Digitale Medien

Take the strain (1982)

Barnstable, Colin J.

[s.l.] : Nature Publishing Group

Nature 299 (1982), S. 504-504

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ISSN: 1476-4687

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Notizen: [Auszug] Journal of Neuroimmunology. Editors-in-chief C.S.Raine and P.O.Behan. 6/yr in 2 vols. (Elsevier Biomedical.) Dfl. 450, $180. THE new Journal of Neuroimmunology (JN) is trying to provide a meeting point for neuropathologists and those who use immunological methods as a tool to study the ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/299504b0

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5

Digitale Medien

The subcellular localization of rat photoreceptor-specific antigens (1983)

Fekete, Donna M. ; Barnstable, Colin J.

Springer

Journal of neurocytology 12 (1983), S. 785-803

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ISSN: 1573-7381

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: Summary The subcellular localization of three photoreceptor antigens (RET-P1, rhodopsin and RET-P2) has been studied by electron microscopic immunocytochemistry of rat retinas. Localization was also examined by determining the amount of RET-P1 and RET-P2 antigen in various subcellular fractions. RET-P1 and RET-P2 antigens were further characterized by immunoblotting of crude retina membrane proteins which had been separated by one-dimensional gel electrophoresis. RET-P1 antigen has been detected with a monoclonal antibody that reacts with the perikarya, inner segments, and outer segments of adult rat photoreceptors by peroxidase immunolabelling of fixed tissue sections. Analysis at the electron microscopic level has shown that RET-P1 antigen is located on the external face of the inner and outer segment plasma membrane. A monoclonal antibody against purified bovine rhodopsin (RHO-C7) labels the outer segments of rat retinas by peroxidase immunocytochemistry. Ultrastructural antibody localization indicates that this particular determinant of rhodopsin is exposed on the external face of the plasma membrane of outer segments and may also be expressed on the surface of the inner segments. RET-P2 antibody labels only the outer segments of adult rat photoreceptors by peroxidase immunocytochemistry. The light microscopic labelling of RET-P2 antibody in the presence, but not in the absence, of detergent suggests that it is an intracellular antigen. The results of both ultrastructural labelling and biochemical fractionation are consistent with the localization of RET-P2 antigen on the internal face of the plasma membrane and/or the cytoplasmic face of the disc membranes. RET-P2 antigen was found to be a protein (or glycoprotein) of apparent molecular weight 38 000 ± 3000.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01258151

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