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1
Modification of hepatic fructose 1,6-diphosphatase activity by proteolytic enzymes and sulfhydryl reagents.
Arch Biochem Biophys. 1971 Sep;146(1):134-43. doi: 10.1016/s0003-9861(71)80049-8.
2
Fructose 1, 6-diphosphatase from liver: isolation of the native form with optimal activity at neutral pH.
Arch Biochem Biophys. 1971 Sep;146(1):161-6. doi: 10.1016/s0003-9861(71)80052-8.
3
Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin.
Arch Biochem Biophys. 1972 Mar;149(1):222-31. doi: 10.1016/0003-9861(72)90317-7.
5
Modification of the catalytic properties of rabbit liver fructose diphosphatase by a particulate fraction from liver.
Arch Biochem Biophys. 1971 Sep;146(1):153-60. doi: 10.1016/s0003-9861(71)80051-6.
7
Conversion of "neutral" to "alkaline" fructose 1,6-diphosphatase by controlled digestion with papain.
Arch Biochem Biophys. 1971 Dec;147(2):762-6. doi: 10.1016/0003-9861(71)90436-x.
8
P-nitrophenyl phosphate as substrate for rabbit liver fructose diphosphatase.
Biochem Biophys Res Commun. 1971 Oct 1;45(1):98-103. doi: 10.1016/0006-291x(71)90055-6.
9
Bovine hepatic fructose 1,6-diphosphatase: -glycerophosphate hydrolysis-evidence for a shared active site.
Arch Biochem Biophys. 1971 Sep;146(1):144-52. doi: 10.1016/s0003-9861(71)80050-4.

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