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
Chemical and biochemical analysis of isolated amyloid fibrils reveals the presence of different classes of proteins which are often related to distinct clinical forms of amyloidosis and are useful to classify the amyloid deposits. In this study, enzymatic digestions using hyaluronidase, chondroitinase AC and B, neuraminidase, and chemical extractions using mild acid hydrolysis with hydrochloric and sulfuric acid, were used to control the specificity of various topooptical reactions. The disappearance of intense staining after these extraction methods indicates that tissue-isolated amyloid fibrils contain sialic acids and glycosaminoglycans (GAGs). We conclude that topooptical reactions are the most sensitive methods to detect conformational changes in the non-fibrillar component of amyloid deposits and tissue-isolated amyloid fibrils.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1016/j.acthis.2006.03.015 | DOI Listing |
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