Using Molecular Beacons To Probe Molecular Interactions between Lactate Dehydrogenase and Single-Stranded DNA

2000 ◽  
Vol 72 (14) ◽  
pp. 3280-3285 ◽  
Author(s):  
Xiaohong Fang ◽  
Jianwei Jeff Li ◽  
Weihong Tan
2018 ◽  
Vol 430 (1) ◽  
pp. 87-101 ◽  
Author(s):  
Yao Fang ◽  
Xiao Xiao ◽  
Shu-Xing Li ◽  
Aaron Wolfe ◽  
Xiaojiang S. Chen

2013 ◽  
Vol 430 (2) ◽  
pp. 466-469 ◽  
Author(s):  
Luigi Fiume ◽  
Marina Vettraino ◽  
Domenica Carnicelli ◽  
Valentina Arfilli ◽  
Giuseppina Di Stefano ◽  
...  

1986 ◽  
Vol 233 (3) ◽  
pp. 913-916 ◽  
Author(s):  
F S Sharief ◽  
S H Wilson ◽  
S S-L Li

A 36,000-Mr protein purified from mouse myeloma on the basis of selective binding to a single-stranded DNA (ssDNA)-cellulose column has been identified as the lactate dehydrogenase A (LDH-A) subunit. A homogeneous preparation of this mouse myeloma ssDNA-binding protein, termed the ‘low-salt-eluting protein’, was found to possess LDH activity, and rabbit antiserum prepared against this protein was shown to cross-react with purified 36,000-Mr LDH-A subunits from mouse and bovine sources. In addition, bovine and human LHD-A4 isoenzymes were shown to be capable of binding ssDNA. These enzymic and immunological identities with LDH-A were not observed with purified helix-destabilizing protein 1 from mouse myeloma. A model for ssDNA-LDH binding is discussed.


Author(s):  
Howard B. Kaiserman ◽  
Ward F. Odenwald ◽  
Deborah J. Stowers ◽  
Everdina H.A. Poll ◽  
Robert M. Benbow

2019 ◽  
Vol 21 (29) ◽  
pp. 16367-16380 ◽  
Author(s):  
Timothy Cholko ◽  
Shivansh Kaushik ◽  
Chia-en A. Chang

Simulations reveal the dynamic properties of freely diffusing and surface-tethered ssDNA on self-assembled monolayers with widely varying surface properties.


The Analyst ◽  
2012 ◽  
Vol 137 (16) ◽  
pp. 3787 ◽  
Author(s):  
Dong-Shan Xiang ◽  
Guo-Hua Zhou ◽  
Ming Luo ◽  
Xing-Hu Ji ◽  
Zhi-Ke He

Author(s):  
Dean A. Handley ◽  
Jack T. Alexander ◽  
Shu Chien

In situ preparation of cell cultures for ultrastructural investigations is a convenient method by which fixation, dehydration and embedment are carried out in the culture petri dish. The in situ method offers the advantage of preserving the native orientation of cell-cell interactions, junctional regions and overlapping configurations. In order to section after embedment, the petri dish is usually separated from the polymerized resin by either differential cryo-contraction or solvation in organic fluids. The remaining resin block must be re-embedded before sectioning. Although removal of the petri dish may not disrupt the native cellular geometry, it does sacrifice what is now recognized as an important characteristic of cell growth: cell-substratum molecular interactions. To preserve the topographic cell-substratum relationship, we developed a simple method of tapered rotary beveling to reduce the petri dish thickness to a dimension suitable for direct thin sectioning.


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