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Cooperative interactions between native and modified subunits of rabbit liver fructose 1,6-bisphosphatase.
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Relationship between thiol group modification and the binding site for fructose 2,6-bisphosphate on rabbit liver fructose-1,6-bisphosphatase.
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Regulation of rabbit liver fructose-1,6-bisphosphatase by metals, nucleotides, and fructose 2,6-bisphosphate as determined from fluorescence studies.
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Purification of human liver fructose-1,6-bisphosphatase.
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Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation.
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The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase.
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Changes in activity and molecular properties of fructose 1, 6-bisphosphatase during fasting and refeeding.
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Changes in rabbit-liver lysosomes and fructose 1,6-bisphosphatase induced by cold and fasting.
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Biochemical observations on a case of hepatic fructose-1,6-diphosphatase deficiency.
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Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.
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The purification of fructose 1,6-diphosphatase from ox liver and its activation by ethylenediaminetetra-acetate.
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Hormonal effects on structure and catalytic properties of fructose 1,6-bisphosphatase.
Proc Natl Acad Sci U S A. 1975 Aug;72(8):2969-73. doi: 10.1073/pnas.72.8.2969.
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Protein measurement with the Folin phenol reagent.
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ALTERATION OF ENZYMATIC ACTIVITIES OF RAT LIVER DIPHOSPHATASE BY TREATMENT WITH PAPAIN OR UREA.
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
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The tryptophan microenvironments in apomyoglobin.
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The carboxyl-terminal structure of rabbit liver aldolase (aldolase B).
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Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin.
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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.
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Chemical modification of the allosteric and catalytic sites of fructose 1,6-diphosphatase.
Proc Natl Acad Sci U S A. 1966 May;55(5):1156-61. doi: 10.1073/pnas.55.5.1156.
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Fructose diphosphatase from rabbit liver. 3. Nature of the groups reactive with dinitrofluorobenzene.
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Fructose diphosphatase from rabbit liver. II. Changes in catalytic properties induced by dinitrofluorobenzene.
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