Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme protein-Reference-Cited by-同舟云学术

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Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme protein

Published:1976-05 Issue:2 Volume:70 Page:638-646
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Dzugaj Andrzej,Chu Douglas K.,El-Dorry Hamza A.,Horecker B.L.,Pontremoli S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference18 articles.

1. Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin

2. Evidence for the modification of fructose 1,6-bisphosphatase by two distinct lysosomal proteases

Cited by 40 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase;Acta Crystallographica Section D Biological Crystallography;2011-11-18

2. Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions;FEBS Letters;2007-03-01

3. Regulation of Fructose-Bisphosphatase Activity;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

4. Mechanism of Action of Fructose 1,6-Bisphosphatase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

5. Different Sensitivities of Mutants and Chimeric Forms of Human Muscle and Liver Fructose- 1,6-Bisphosphatases towards AMP;Biological Chemistry;2003-01-27

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