Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP-AMP transphosphorylases from muscle and liver.-Reference-Cited by-同舟云学术

Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP-AMP transphosphorylases from muscle and liver.

Published:1983-02 Issue:3 Volume:258 Page:1901-1907
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kuby S A,Fleming G,Frischat A,Cress M C,Hamada M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Studies on adenosine triphosphate transphosphorylases XIV. Equilibrium binding properties of the crystalline rabbit and calf muscle ATP-AMP transphosphorylase (adenylate kinase) and derived peptide fragments

2. Adenosine Triphosphate-Adenosine 5'-Monophosphate Phosphotransferase of Bovine Liver Mitochondria

3. Rat Liver Adenosine Triphosphate:Adenosine Monophosphate Phosphotransferase Activity

4. Purification of rat liver adenylate kinase isozyme II and comparison with isozyme III

5. Nucleotide Transphosphorylases from Liver

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