Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 143
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 143
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 209
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 994
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3134
Function: GetPubMedArticleOutput_2016
File: /var/www/html/application/controllers/Detail.php
Line: 574
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 488
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
The aqueous and ethanolic extracts of Lippia sidoides Cham. were chemically characterized and tested for their action on enzymes involved in processes such as inflammation, blood coagulation, and digestion. Both extracts potentiated the activity of phospholipases A present in the venom of Bothrops atrox in 12 % and completely inhibited the hemolysis induced by B. jararacussu and B. moojeni venoms in the proportions between 1 : 0.5 and 1 : 5 (venom/extracts (w/w)). They inhibited the thrombolysis induced by B. moojeni (10 to 25 %), potentiated the thrombolysis induced by the Lachesis muta muta venom (30 to 80 %), prolonged the coagulation time induced by B. moojeni and L. muta muta venoms, and presented antigenotoxic action. Both extracts reduced the activity of α-glycosidases, the aqueous extract inhibited lipases, and the ethanolic extract inhibited α-amylases. The results demonstrate the modulatory action of the extracts on proteases, phospholipases, and digestive enzymes. In addition, the rich phenolic composition of these extracts highlights their potential for nutraceutical use.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1002/cbdv.201800558 | DOI Listing |
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