Spectrophotometric investigations of the interaction of native and chemically modified ATP:guanidinophosphotransferases with their substrates (Q71542865)

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scientific article published on June 10, 1970

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English	Spectrophotometric investigations of the interaction of native and chemically modified ATP:guanidinophosphotransferases with their substrates	scientific article published on June 10, 1970

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scholarly article

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19 October 2019

Spectrophotometric investigations of the interaction of native and chemically modified ATP: guanidinophosphotransferases with their substrates (English)

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Europe PubMed Central

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19 October 2019

Spectrophotometric investigations of the interaction of native and chemically modified ATP:guanidinophosphotransferases with their substrates (English)

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10.1016/0005-2744(70)90153-1

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20 May 2023

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C. Roustan

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20 May 2023

L. A. Pradel

2

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20 May 2023

R. Kassab

3

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20 May 2023

A. Fattoum

4

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20 May 2023

N. V. Thoai

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20 May 2023

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publication date

1 June 1970

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19 October 2019

10 June 1970

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=5459548

20 May 2023

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11

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10.1016/0005-2744(70)90153-1

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20 May 2023

https://api.elsevier.com/content/article/PII:0005274470901531?httpAccept=text/plain

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10.1016/0005-2744(70)90153-1

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20 May 2023

Biochimica et Biophysica Acta

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19 October 2019

206

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19 October 2019

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19 October 2019

369-379

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19 October 2019

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

1

1 reference

10.1016/0005-2744(70)90153-1

https://api.crossref.org/works/10.1016/0005-2744(70)90153-1

20 May 2023

Comparative study of the reactive SH groups of ATP: guanidine phosphotransferases

2

1 reference

10.1016/0005-2744(70)90153-1

https://api.crossref.org/works/10.1016/0005-2744(70)90153-1

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The active site of ATP: guanidine phosphotransferases. II. Evidence for an essential histidine residue through use of diethylpyrocarbonate

3

1 reference

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Active site of ATP: guanidine phosphotransferases. I. Reaction of the essential epsilon-NH2 lysine groups with 1-dimethylaminonapthalene-5-sulphonyl chloride

4

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A functional tyrosyl residue in arginine kinase, studied by nitration with tetranitromethane

5

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Ultraviolet absorption spectra of adenosine-5'-triphosphate and related 5'-ribonucleotides

6

1 reference

10.1016/0005-2744(70)90153-1

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ATP:Taurocyamine et ATP:Lombricine phosphotransférases purification et étude des groupements SH

15

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The active centre of chymotrypsin. I. Labelling with a fluorescent dye.

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Biochimica et Biophysica Acta

17

89

255

author name string

Pradel

publication date

1964

1 reference

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Nature of enzyme-coenzyme interactions in liver alcohol dehydrogenase

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Bovine pancreatic ribonuclease-spectrophotometric investigations of the interaction of the enzyme with nucleotides

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An analysis of perturbations in the ultraviolet absorption spectra of proteins and model compounds

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STUDIES ON LIVER ALCOHOL DEHYDROGENASE COMPLEXES. IV. SPECTROPHOTOMETRIC OBSERVATIONS ON THE ENZYME COMPLEXES

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Magnetic Resonance and Kinetic Studies on the Manganese Activated Arginine Kinase Reaction

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Identifiers

10.1016/0005-2744(70)90153-1

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:5459548%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:5459548%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

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