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
Solutions of purified brevin were applied to skinned thin bundles or isolated fibres of smooth muscle. This produced a sharp drop of isometric tension, an effect due to the severing effect of brevin on actin filaments, partially depleted from tropomyosin in skinned preparations. On skinned single fibres, brevin accelerates the speed of unloaded shortening. As no effect was detected on the myofibrillar ATPase turnover rate, brevin was thought to affect the viscosity of the cytoplasm. This was confirmed by analysis of the cytoplasm stiffness which decreased in the presence of brevin. It is proposed that Ca-activated brevin acts on actin-filamin gels, set in parallel to the contractile apparatus.
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Source |
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http://dx.doi.org/10.1007/978-1-4615-2872-2_19 | DOI Listing |
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