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The article discusses the concept of the "Golden Thread of Information" in the construction industry, which emphasizes the need for accurate and up-to-date information throughout a building's lifecycle to ensure safety and compliance with building regulations. The article highlights the importance of maintaining cohesive digital records and using software solutions like Knauf Planner Suite - System Finder to facilitate the storage and access of information. The implementation of the Golden Thread of Information was prompted by the Grenfell Tower tragedy in 2017 and the subsequent establishment of the Building Safety Act, which aims to enhance information processing and sharing in the construction sector. [Extracted from the article]

Myosin from chicken intestinal brush borders is phosphorylated on its heavy chains at threonine by a kinase isolated from brush borders. In contrast to other heavy chain kinases, the brush border kinase activity is dependent on calcium and calmodulin. The partially purified preparation also phosphorylated myosin on its light chains at serine, but in a calmodulin-independent manner. Phosphorylation of the light chains in the absence of calmodulin or both heavy and light chains in the presence of calmodulin activated its actinactivated ATPase activity about 10-fold, to about 50 nmolminper mg.

A calmodulin-independent kinase isolated from chicken intestinal brush border phosphorylates brush border myosin mainly at an apparently single threonine on its 20 kDa light chains. Phosphorylation to 1.9 mol phosphate/mol myosin activated the myosin actin-activated ATPase about 12-fold, to about 100 nmol/min per mg. Brush border myosin ATPase can thus be activated by phosphorylation either at threonine, by calmodulin-independent kinase, or at serine, by calmodulin-dependent myosin light chain kinase, as previously shown [(1987) FEBS Lett. 223, 262–266].

Calmodulin‐dependent myosin light chain kinase isolated from chicken intestinal brush border phosphorylates brush border myosin at an apparently single serine identical to that phosphorylated by smooth muscle myosin light chain kinase. Phosphorylation to 1.8 mol phosphate/mol myosin activated the myosin actin‐activated ATPase about 10‐fold, to about 50 nmol/min per mg. Myosin phosphorylated on its light chains could then be further phosphorylated to a total of 3.2 mol phosphate per mol by brush border calmodulin‐dependent heavy chain kinase. Heavy chain phosphorylation did not alter the actin‐activated ATPase of either myosin prephosphorylated on its light chains or of unphosphorylated myosin.

Several letters to the editor are presented in response to articles in previous issues including "Penalized for Working" in the January 2015 issue, "Controlling Your Opioids" in the January 2015 issue and "Accessible Living Before Its Time" in the January 2015 issue.