You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output.
Click here to find out more.
Mendeley readers
| Chapter title |
Assay of Arginyltransferase Activity by a Fluorescent HPLC Method.
|
|---|---|
| Chapter number | 12 |
| Book title |
Protein Arginylation
|
| Published in |
Methods in molecular biology, January 2015
|
| DOI | 10.1007/978-1-4939-2935-1_12 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2934-4, 978-1-4939-2935-1
|
| Authors |
Koichi Takao |
| Editors |
Anna S. Kashina |
| Abstract |
Syntheses of fluorescent substrate and product for arginyltransferase, N-aspartyl-N'-dansylamido-1,4-butanediamine (Asp-4DNS), and N-arginylaspartyl-N'-dansylamido-1,4-butanediamine (ArgAsp-4DNS), respectively, including their precursor 4-dansylamidobutylamine (4DNS), are described. Then, HPLC conditions are summarized for a baseline separation of the three compounds in 10 min. The present method, which permits the simultaneous determination of Asp-4DNS, 4DNS, and ArgAsp-4DNS (in eluting order), is advantageous in measuring arginyltransferase activity and detecting the unfavorable enzyme(s) in 105,000 × g supernatant of tissues to ensure accurate determination. |
Mendeley readers
The data shown below were compiled from readership statistics for 2 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 2 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Lecturer | 1 | 50% |
| Unknown | 1 | 50% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 1 | 50% |
| Unknown | 1 | 50% |