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Solubilization and partial purification of cholinephosphotransferase in hamster tissues
Author(s) -
O Karmin,
Choy Patrick C.
Publication year - 1990
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02562217
Subject(s) - lipidology , clinical chemistry , hamster , chromatography , chemistry , solubilization , mesocricetus , biochemistry , biology , microbiology and biotechnology
CDP choline:1,2‐diacylglycerol cholinephosphotransferase (EC 2.7.8.2) is located on the cytoplasmic side of the endoplasmic reticulum, and catalyzes the final step in the synthesis of phosphatidylcholine via the CDP choline pathway. The enzyme was solubilized from hamster liver microsomes by 3% Triton QS‐15, and partially purified by DEAE‐Sepharose chromatography and Sepharose 6B chromatography. The microsomal and partially purified enzymes displayed similar pH profile, and both showed absolute requirement for Mg ++ or other divalent cations. The Km values of CDP choline were similar between microsomal and partially purified enzyme, whereas the Km value for diacylglycerol was substantially lowered when the enzyme was partially purified. Hamster heart cholinephosphotransferase was not solubilized by Triton QS‐15.