Literature DB >> 5729948

[Interaction of ATP:guanidine phosphotransferases with their substrates, studies by differential spectrophotometry].

C Roustan, R Kassab, L A Pradel, N van Thoai.   

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Year:  1968        PMID： 5729948     DOI： 10.1016/0005-2744(68)90212-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


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  4 in total

1.  Evolutionary variation between a monomer and a dimer arginine kinase. Purification of the enzyme from Holothuria forskali and a comparison of some properties with that from Homarus vulgaris.

Authors:  E O Anosike; B H Moreland; D C Watts
Journal:  Biochem J       Date:  1975-03       Impact factor: 3.857

2.  The use of arginine analogues for investigating the functional organization of the arginine-binding site in lobster muscle arginine kinase. Role of the 'essential' thiol group.

Authors:  D C Watts; E O Anosike; B Moreland; R J Pollitt; C R Lee
Journal:  Biochem J       Date:  1980-03-01       Impact factor: 3.857

3.  Effects of arginine and some analogues of the partial adenosine triphosphate-adenosine diphosphate exchange reaction catalysed by arginine kinase. Evolutionary divergence in the mechanism of action of a monomer and a dimer arginine kinase.

Authors:  E O Anosike; D C Watts
Journal:  Biochem J       Date:  1976-06-01       Impact factor: 3.857

4.  Properties and mechanism of action of creatine kinase from ox smooth muscle. Anion effects compared with pyruvate kinase.

Authors:  B Focant; D C Watts
Journal:  Biochem J       Date:  1973-10       Impact factor: 3.857
  4 in total

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