Identification of peptides from the adenine binding domains of ATP and AMP in adenylate kinase: isolation of photoaffinity-labeled peptides by metal chelate chromatography-Reference-Cited by-同舟云学术

Identification of peptides from the adenine binding domains of ATP and AMP in adenylate kinase: isolation of photoaffinity-labeled peptides by metal chelate chromatography

Published:1992-05-12 Issue:18 Volume:31 Page:4479-4487
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Salvucci Michael E.,Chavan Ashok J.,Haley Boyd E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00133a014

Reference32 articles.

1. Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography

2. Protein-electroblotting and -microsequencing strategies in generating protein data bases from two-dimensional gels.

3. Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.

4. Tautomerism of 2-azidoadenine nucleotides Effects on enzyme kinetics and photoaffinity labeling

5. The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution

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