Multiple chromatographic forms of ATP citrate lyase from rat liver
نویسندگان
چکیده
منابع مشابه
Structure of ATP Citrate Lyase from Rat Liver
ATP citrate lyase was purified by two different procedures from the livers of’ rats first starved and then fed with a fat-deficient and high carbohydrate-glycerol diet. These enzyme preparations were judged homogeneous by sedimentation equilibrium and polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was around 4.4 x 105 as determined hy sedimentation equilibrium. On...
متن کاملStructure of ATP citrate lyase from rat liver. Physicochemical studies and proteolytic modification.
ATP citrate lyase was purified by two different procedures from the livers of rats first starved and then fed with a fat-deficient and high carbohydrate-glycerol diet. These enzyme preparations were judged homogeneous by sedimentation equilibrium and polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was around 4.4 X 10(5) as determined by sedimentation equilibrium. O...
متن کاملACLY (ATP citrate lyase)
Other names: ACL, ATPCL, CLATP HGNC (Hugo): ACLY Location: 17q21.2 Note Note that the International Union for Biochemistry and Molecular Biology (IUBMB)'s enzyme nomenclature accepts ATP citrate synthase as the name for ACLY's encoded protein (EC 2.3.3.8). However, ATP citrate lyase is more commonly used and other names include citrate cleavage enzyme, ATP-citrate (pro-S)-lyase, ATPCL, CLATP. A...
متن کاملBinding of ATP citrate lyase to the microsomal fraction of rat liver.
Purified rat liver ATP citrate lyase is shown to bind to the microsomal fraction of rat liver. Under the same conditions the enzyme does not bind significantly to the mitochondrial fraction or to the outer membrane prepared from the mitochondrial fraction. The binding component of the microsomal fraction is further identified as the endoplasmic reticulum, and a protein component of the membrane...
متن کاملEvidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver.
Rat liver ATP citrate lyase was inactivated by 2, 3-butanedione and phenylglyoxal. Phenylglyoxal caused the most rapid and complete inactivation of enzyme activity in 4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid buffer, pH 8. Inactivation by both butanedione and phenylglyoxal was concentration-dependent and followed pseudo- first-order kinetics. Phenylglyoxal also decreased autophosphor...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1983
ISSN: 0306-3283
DOI: 10.1042/bj2140299