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
Hydrolysis of modified walleye pollock protein under the action of pepsin pancreatic and intestinal enzymes was studied under conditions in vitro and in vivo. It was found that the degree of dissolution of bonds is decreased in the experiments in vitro by 18.05-24.87%, in vivo by 34.2%, as compared to the experiments where casein was used. At the same time hydrolysis of oligo- and dipeptides realized in the intestine by amino- and dipeptidases is stimulated under the influence of the pollock protein by 16.07-53.7%. Therefore it is suggested that utilization of the protein studied depends on the capacity of peptidases to release dipeptides in separate acetylated or free dipeptides. Thus, for the sake of regulatory and adaptive changes of secretion of some digestive glands and especially enzymes, fixed on enterocyte brush edge, the necessary enzyme-substrate correspondence is provided, as a result of which hydrolysis of the pollock protein is achieved.
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