Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin: Sites of cleavage and activity of the modified enzyme
- 1 December 1977
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 184 (2), 535-545
- https://doi.org/10.1016/0003-9861(77)90463-5
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisinArchives of Biochemistry and Biophysics, 1977
- Rabbit liver fructose 1,6-bisphosphatase: The sequence of the amino-terminal regionArchives of Biochemistry and Biophysics, 1977
- Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme proteinBiochemical and Biophysical Research Communications, 1976
- Reaction of peptides with fluorescamine on paper after chromatography or electrophoresisAnalytical Biochemistry, 1975
- Studies on the structure of rabbit muscle aldolaseArchives of Biochemistry and Biophysics, 1975
- Use of fluorescamine in the chromatographic analysis of peptides from proteinsAnalytical Biochemistry, 1974
- Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisinArchives of Biochemistry and Biophysics, 1972
- Fructose 1, 6-diphosphatase from liver: Isolation of the native form with optimal activity at neutral pHArchives of Biochemistry and Biophysics, 1971
- Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide GroupsNature, 1966
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958