Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Mushroom tyrosinase from (TYR) is often used during the development of tyrosinase inhibitors for medicinal and cosmetic purposes. In the search for novel tyrosinase inhibitors, this study identified hematoxylin as an alternative substrate for TYR. The interaction of hematoxylin with TYR was investigated through spectrophotometric and chromatographic analyses. The results showed that hematoxylin acted as an TYR substrate and exhibited Michaelis-Menten kinetic behaviour at concentrations below 1.25 mM. The substrate properties of hematoxylin were similar to the natural tyrosinase substrate, L-3,4-dihydroxyphenylalanine (L-DOPA), with regards to K, while V was eightfold lower. The main oxidation product formed during the reaction of TYR with hematoxylin was identified as hematein. This is the first report of the interaction of hematoxylin with TYR.
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Source |
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http://dx.doi.org/10.1055/a-2381-5201 | DOI Listing |
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