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: Differential solubilization of rabbit liver plasma membrane gamma-glutamyltransferase by proteases and detergents: effect of phenobarbital treatment.
    Author: Ratanasavanh D, Houssier M, Galteau MM, Siest G.
    Journal: Clin Chim Acta; 1984 Dec 29; 144(2-3):127-32. PubMed ID: 6152203.
    Abstract:
    In an attempt to understand the mechanism of gamma-glutamyltransferase transfer from the liver to the plasma, potassium chloride, sodium dodecyl sulfate and proteases (papain and bromelain) were used to solubilize rabbit liver plasma membrane gamma-glutamyltransferase. Potassium chloride solutions solubilized 10-30% of membrane proteins but only 1-3% of membrane gamma-glutamyltransferase activity. However, when sodium dodecyl sulfate is used, even at low concentration (0.1-0.2%, w/v) greater than 90% of membrane gamma-glutamyltransferase activity and about 80% of membrane proteins can be solubilized. Furthermore, we showed that unlike the effect of bile salts on the membrane gamma-glutamyltransferase of phenobarbital-treated animals, the same treatment seems to have no influence on membrane gamma-glutamyltransferase solubilization by proteases. Indeed, the ratios of gamma-glutamyltransferase solubilization by papain or bromelain were the same for liver membranes obtained from control and phenobarbital-treated animals.
    [Abstract] [Full Text] [Related] [New Search]