• Login
    View Item 
    •   Home
    • Colleges & Programs
    • Medical College of Georgia (MCG)
    • Department of Cellular Biology and Anatomy
    • Department of Cellular Biology and Anatomy: Faculty Research and Presentations
    • View Item
    •   Home
    • Colleges & Programs
    • Medical College of Georgia (MCG)
    • Department of Cellular Biology and Anatomy
    • Department of Cellular Biology and Anatomy: Faculty Research and Presentations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of Scholarly CommonsCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjects

    My Account

    LoginRegister

    About

    AboutCreative CommonsAugusta University LibrariesUSG Copyright Policy

    Statistics

    Display statistics

    ONTOGENETIC CHANGES OF PROTEINS OF ENDOPLASMIC RETICULUM

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    733.pdf
    Size:
    488.4Kb
    Format:
    PDF
    Download
    Authors
    Black, Owen
    Bresnick, Edward
    Issue Date
    1972-03-1
    URI
    http://hdl.handle.net/10675.2/540
    
    Metadata
    Show full item record
    Abstract
    The proteins of the smooth and rough endoplasmic reticulum from fetal, immature, and adult male rats were compared after incorporation of two radioactively labeled precursors, 14C-labeled amino acids and δ-aminolevulinic acid-3H by means of gel electrophoresis. The labeling patterns indicated that protein components present in two major electrophoretic bands underwent significant synthesis in fetal tissue while three actively incorporating protein bands were noted in adult tissue. Although the uptake of the amino acids-14C decreased for the smooth and rough elements of the endoplasmic reticulum as a whole during liver development, the qualitative patterns were not significantly different in adult and fetal livers. The over-all incorporation (disintegrations per minute per milligram protein) of the heme precursor into the smooth and rough elements also did not change with development. However, a change was noted in the distributional electrophoretic patterns with development. The estimation of molecular weight (by disc electrophoresis) and the incorporation of the heme precursor suggested the similarity of the two major protein bands to cytochrome P-450 and cytochrome b5, components of the endoplasmic reticulum, thought to be involved in the mixed-function oxidase system. The evidence indicated that in fetal liver, at a time when the oxidase capability was low, the amino acid incorporation into these two protein groups was the same as in the adult. The incorporation of the heme moiety, however, was different, decreasing in the cytochrome b5 region and increasing in the cytochrome P-450 region during development. These results correlate with the increase in oxidase activity associated with liver development.
    Citation
    J Cell Biol. 1972 Mar 1; 52(3):733-742
    Collections
    Department of Cellular Biology and Anatomy: Faculty Research and Presentations

    entitlement

     
    DSpace software (copyright © 2002 - 2021)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.