Fluorescence energy transfer between cysteine 199 and cysteine 343: evidence for magnesium ATP-dependent conformational change in the catalytic subunit of cAMP-dependent protein kinase-Reference-Cited by-同舟云学术

Fluorescence energy transfer between cysteine 199 and cysteine 343: evidence for magnesium ATP-dependent conformational change in the catalytic subunit of cAMP-dependent protein kinase

Published:1989-04-18 Issue:8 Volume:28 Page:3606-3613
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

First Eric A.,Johnson David A.,Taylor Susan S.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00434a068

Reference28 articles.

1. Sulfhydryl group reactivity of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart: a probe of holoenzyme structure

2. Adenosine cyclic 3',5'-monophosphate dependent protein kinase: nucleotide binding to the chemically modified catalytic subunit

3. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

4. Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates.

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