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Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour...

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b8e86b9d978a4f3794c48f61ddadd69d

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

About this item

Full title

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

Publisher

Switzerland: MDPI AG

Journal title

Biomolecules (Basel, Switzerland), 2018-08, Vol.8 (3), p.79

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences. Our previous observations suggested that the metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1)...

Alternative Titles

Full title

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_b8e86b9d978a4f3794c48f61ddadd69d

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b8e86b9d978a4f3794c48f61ddadd69d

Other Identifiers

ISSN

2218-273X

E-ISSN

2218-273X

DOI

10.3390/biom8030079

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