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
When a female mosquito takes a blood meal, proteolytic activity surges in the midgut. Trypsin-like serine proteases are the major endoproteolytic enzyme induced by feeding in mosquitoes. The mosquito midgut lacks trypsin activity before the blood meal, but in most anautogenous mosquitoes, trypsin activity increases continuously up to 30 h after feeding and subsequently returns to baseline levels by 60 h. Trypsin activity in mosquitoes is restricted entirely to the posterior midgut lumen, where blood is stored and digested. Trypsin enzyme activity can be quantitatively measured using the artificial α-benzoyl--arginine 4-nitroanilide hydrochloride substrate, a method described in our associated protocol.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1101/pdb.top107656 | DOI Listing |
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