Open AccessImmunochemical Studies on Rat‐Liver Microsomal NAD Glycohydrolase
Author(s) -
Bock Karl Walter,
Matern Siegfried
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03027.x
Subject(s) - microsome , sephadex , nad+ kinase , biochemistry , antiserum , enzyme , chemistry , chromatography , microbiology and biotechnology , membrane , antibody , biology , immunology
Rabbit antiserum was prepared against rat liver microsomal NAD glycohydrolase solubilized by lipase treatment and subsequently purified by successive DEAE‐cellulose, Sephadex G‐100 chromatography and polyacrylamide gel electrophoresis. The antibody inhibited the purified enzyme 60–80%, but the membrane‐bound and Triton X‐100 solubilized enzyme up to 20–30% only. A single precipitation line was produced when the antibody reacted with the purified enzyme, and with crude lipase and Triton X‐100 solubilized enzyme preparations. NAD glycohydrolase from liver rough‐microsomal and plasma‐membrane fractions reacted identically. The antibody to rat liver NAD glycohydrolase similarly inhibited the lipase or Triton X‐100 solubilized and membrane‐bound NAD glycohydrolase from rat spleen and brain as well as from mouse liver but not from bovine liver.