These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Intracellular protein breakdown. VIII. The use of double-labeled proteins as substrates].
    Author: Bohley P, Kirschke H, Langner J, Wiederanders B, Ansorge S.
    Journal: Acta Biol Med Ger; 1976; 35(3-4):301-7. PubMed ID: 970040.
    Abstract:
    Double-labeled proteins from rat liver cytosol (14C in long-lived, 3H in short-lived proteins after in-vivo-labeling) are used as substrates for unlabeled proteinases in vitro. Differences in the degradation rates of short-lived and long-lived proteins in vitro by different proteinases and after addition of different effectors allow conclusions concerning their importance for the in-vivo-turnover of substrate proteins. The main activity (greater than 90%) of soluble-lysosomal proteinases at pH 6,1 and pH 6,9 is caused by thiolproteinases, which degrade preferentially short-lived cytosol proteins. These proteinases are inhibited by leupeptin. Autolysis of double-labeled cell fractions shows a remarkably faster breakdown of short-lived substrate proteins only in the soluble part of lysosomes. Microsomal fractions degrade in vitro preferentially long-lived substrate proteins.
    [Abstract] [Full Text] [Related] [New Search]