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: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
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
AGG, the codon of 122 Arg of trichosanthin (TCS) was mutated to GGG (Gly) by U-DNA site-directed mutagenesis. The mutant TCS was expressed and purified from the supernatant of host cells, its activities were assayed and compared with expressed wild-type TCS. The results showed that the R122G TCS was still active as a RNA N-glycosidase but its ability to inhibit protein synthesis was 160-fold less than that of wild-type TCS, its abortifacient ability on mid-term gestated mice reduced from 100% to 9.3%, which suggested that 122 Arg was indirectly involved in the catalysis, and it played an important role in its bioactivities.
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