Information Tradeoff Relations for Finite-Strength Quantum Measurements

In this paper we give a new way to quantify the folklore notion that quantum measurements bring a disturbance to the system being measured. We consider two observers who initially assign identical mixed-state density operators to a two-state quantum system. The question we address is to what extent one observer can, by measurement, increase the purity of his density operator without affecting the purity of the other observer's. If there were no restrictions on the first observer's measurements, then he could carry this out trivially by measuring the initial density operator's eigenbasis. If, however, the allowed measurements are those of finite strength---i.e., those measurements strictly within the interior of the convex set of all measurements---then the issue becomes significantly more complex. We find that for a large class of such measurements the first observer's purity increases the most precisely when there is some loss of purity for the second observer. More generally the tradeoff between the two purities, when it exists, forms a monotonic relation. This tradeoff has potential application to quantum state control and feedback.Comment: 15 pages, revtex3, 3 eps figure

Recombinant Expression, Purification, and Functional Characterisation of Connective Tissue Growth Factor and Nephroblastoma-Overexpressed Protein

The CCN family of proteins, especially its prominent member, the Connective tissue growth factor (CTGF/CCN2) has been identified as a possible biomarker for the diagnosis of fibrotic diseases. As a downstream mediator of TGF-β1 signalling, it is involved in tissue scarring, stimulates interstitial deposition of extracellular matrix proteins, and promotes proliferation of several cell types. Another member of this family, the Nephroblastoma-Overexpressed protein (NOV/CCN3), has growth-inhibiting properties. First reports further suggest that these two CCN family members act opposite to each other in regulating extracellular matrix protein expression and reciprocally influence their own expression when over-expressed. We have established stable HEK and Flp-In-293 clones as productive sources for recombinant human CCN2/CTGF. In addition, we generated an adenoviral vector for recombinant expression of rat NOV and established protocols to purify large quantities of these CCN proteins. The identity of purified human CCN2/CTGF and rat CCN3/NOV was proven by In-gel digest followed by ESI-TOF/MS mass spectrometry. The biological activity of purified proteins was demonstrated using a Smad3-sensitive reporter gene and BrdU proliferation assay in permanent cell line EA•hy 926 cells. We further demonstrate for the first time that both recombinant CCN proteins are N-glycosylated