77Se NMR Investigation of the K(x)Fe(2-y)Se(2) High Tc Superconductor (Tc=33K)

We report a comprehensive 77Se NMR study of the structural, magnetic, and superconducting properties of a single crystalline sample of the newly discovered FeSe-based high temperature superconductor K(x)Fe(2-y)Se(2) (Tc=33K) in a broad temperature range up to 290 K. We will compare our results with those reported for FeSe (Tc=9K) and FeAs-based high Tc systems.Comment: Final versio

NMR Characterization of Sulphur Substitution Effects in the K(x)Fe(2-y)Se(2-z)S(z) high Tc Superconductor

We present an NMR study of the effect of S substitution in the high Tc superconductor K(x)Fe(2-y)Se(2-z)S(z) in a temperature range up to 250 K. We present NMR Knight shift and nuclear spin-lattice relaxation rate 1/T1 data, and compare our results to that of the non-substituted system K(x)Fe(2-y)Se(2).Comment: Typos fixed, figure replace

Entropic Inequalities for a Class of Quantum Secret Sharing States

It is well-known that von Neumann entropy is nonmonotonic unlike Shannon entropy (which is monotonically nondecreasing). Consequently, it is difficult to relate the entropies of the subsystems of a given quantum state. In this paper, we show that if we consider quantum secret sharing states arising from a class of monotone span programs, then we can partially recover the monotonicity of entropy for the so-called unauthorized sets. Furthermore, we can show for these quantum states the entropy of the authorized sets is monotonically nonincreasing.Comment: LaTex, 5 page

Identification of a carbohydrate-based endothelial ligand for a lymphocyte homing receptor.

Lymphocyte attachment to high endothelial venules within lymph nodes is mediated by the peripheral lymph node homing receptor (pnHR), originally defined on mouse lymphocytes by the MEL-14 mAb. The pnHR is a calcium-dependent lectin-like receptor, a member of the LEC-CAM family of adhesion proteins. Here, using a soluble recombinant form of the homing receptor, we have identified an endothelial ligand for the pnHR as an approximately 50-kD sulfated, fucosylated, and sialylated glycoprotein, which we designate Sgp50 (sulfated glycoprotein of 50 kD). Recombinant receptor binding to this lymph node-specific glycoprotein requires calcium and is inhibitable by specific carbohydrates and by MEL-14 mAb. Sialylation of the component is required for binding. Additionally, the glycoprotein is precipitated by MECA-79, an adhesion-blocking mAb reactive with lymph node HEV. A related glycoprotein of approximately 90 kD (designated as Sgp90) is also identified

No-Cloning Theorem on Quantum Logics

This paper discusses the no-cloning theorem in a logico-algebraic approach. In this approach, an orthoalgebra is considered as a general structure for propositions in a physical theory. We proved that an orthoalgebra admits cloning operation if and only if it is a Boolean algebra. That is, only classical theory admits the cloning of states. If unsharp propositions are to be included in the theory, then a notion of effect algebra is considered. We proved that an atomic Archimedean effect algebra admitting cloning operation is a Boolean algebra. This paper also presents a partial result indicating a relation between cloning on effect algebras and hidden variables.Comment: To appear in J. Math. Phy

Multilevel Block Coded Modulation with Unequal Error Protection

Multilevel block coded modulation (BCM) schemes with unequal error protection (UEP) are investigated. These schemes are based on unconventional set partitions that greatly reduce the error coefficients associated with multi-stage decoding of conventional BCM, at the expense of smaller intra-set distances

A homing receptor-IgG chimera as a probe for adhesive ligands of lymph node high endothelial venules.

The binding of lymphocytes to high endothelial venules (HEV) within peripheral lymph nodes (pln) is thought to be mediated by a lectinlike adhesion molecule termed the pln homing receptor (pln HR). The cloning and sequencing of cDNAs encoding both murine and human pln HR revealed that these adhesion molecules contain protein motifs that are homologous to C-type or calcium dependent lectin domains as well as to epidermal growth factor (egf) and complement-regulatory protein domains. We have produced a novel, antibody-like form of the murine HR by joining the extracellular region of the receptor to a human IgG heavy chain. This antibody-like molecule is capable of recognizing carbohydrates, blocking the binding of lymphocytes to pln HEV, and serving as a histochemical reagent for the staining of pln HEV. This murine HR-IgG chimera should prove useful in analyzing the distribution of the HR ligand(s) in normal as well as in inflammatory states

The complement binding-like domains of the murine homing receptor facilitate lectin activity.

The leukocyte homing receptor (HR), the endothelial leukocyte adhesion molecule, and gmp140/platelet activation-dependent granule membrane protein are members of a family of adhesion molecules, termed the lectin cell adhesion molecules (LEC-CAMS) which are unified by a multi-domain structure containing a lectin motif, an epidermal growth factor-like (egf) motif, and variable numbers of a complement binding-like (CB) motif. Previous data have indicated a predominant role for the lectin motif in cell adhesion directed by the LEC-CAMS, although the egf-like domain of the HR may also play a potential role in cell binding. While the role(s) of the CB domains in the LEC-CAMS is currently not understood, they have been hypothesized to act as rigid spacers or stalks for lectin and perhaps, egf domain presentation. In this paper, we analyze the functional characteristics of murine HR-IgG chimeras containing the lectin, lectin plus egf, and lectin plus egf plus CB domains. The Mel 14 mAb, an adhesion blocking antibody which recognizes a conformational determinant in the N-terminus of the HR lectin domain, shows a significantly decreased affinity for a HR construct which lacks the CB motifs, consistent with the possibility that the CB domains are involved with lectin domain structure. In agreement with this conjecture, HR mutants lacking the CB domains show a profound decrease in lectin-specific interaction with the carbohydrate polyphosphomannan ester, suggesting that the changes in Mel 14 affinity for the lectin domain are reflected in lectin functionality. Various assays investigating the interactions between the HR deletion mutants and the peripheral lymph node high endothelium, including cell blocking, immunohistochemical staining, and radioactively labeled ligand binding, all showed that removal of the CB domains results in a lack of HR adhesive function. These results imply that the CB domains of the HR, and, by analogy, the other members of the LEC-CAM family, may play important structural roles involving induction of lectin domain conformation and resultant functionality