A Possible Crypto-Superconducting Structure in a Superconducting Ferromagnet

We have measured the dc and ac electrical and magnetic properties in various magnetic fields of the recently reported superconducting ferromagnet RuSr2GdCu2O8. Our reversible magnetization measurements demonstrate the absence of a bulk Meissner state in the compound below the superconducting transition temperature. Several scenarios that might account for the absence of a bulk Meissner state, including the possible presence of a sponge-like non-uniform superconducting or a crypto-superconducting structure in the chemically uniform Ru-1212, have been proposed and discussed.Comment: 8 pages, 5 PNG figures, submitted to Proceedings of the 9th Japan-US Workshop on High-Tc Superconductors, Yamanashi, Japan, October 13-15, 1999; accepted for publication in Physica C (December 24, 1999

Interaction of linear manno-oligosaccharides with three mannose-specific bulb lectins. Comparison with mannose/glucose-binding lectins

Three new mannose-binding lectins, isolated from daffodil (NPA), amaryllis (HHA), and snowdrop (GNA) bulbs, are capable of precipitating with a linear mannopentaose (Man[alpha]1-3Man[alpha]1-3Man[alpha]1-3Man[alpha]1-2Man). NPA and HHA reacted strongly with the mannopentaose whereas GNA gave a precipitate only at concentrations> 500 [mu]M. A phosphate group at C-6 of the nonreducing terminal mannosyl group prevented precipitation in all three cases. The reduced (NaBH4) mannopentaose, Man4Man-ol, did not precipitate with GNA or NPA, but was active with HHA. This activity was lost when Man4Man-ol was converted (NaIO4 then NaBH4; mild acid hydrolysis of the reduced product) into trisaccharide derivatives. With [alpha]--Manp-OMe the three lectins gave UV difference spectra having large positive peaks at 292-293 and 283-284 nm, and a small positive peak at 275 nm, characteristic of tryptophanyl and tyrosyl residues. The association constants for the interaction with [alpha]--Manp-OMe were very low (NPA, 86; HHA, 66; and GNA, 41 M-1), but the lectins bound methyl (1 --> 3)-[alpha]-mannobioside with increased affinity (K for NPA 540, for HHA 2400, and for GNA 200 M-1). The bulb lectins lack binding sites for hydrophobic ligands, as judged by their failure to interact with the fluorescent probes 8-anilino-1-naphthalensulfonic acid (ANS) and 6-p-toluidino-2-naphthalenesulfonic acid (TNS).Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/30043/1/0000411.pd

Advances in Electronic-Nose Technologies Developed for Biomedical Applications

The research and development of new electronic-nose applications in the biomedical field has accelerated at a phenomenal rate over the past 25 years. Many innovative e-nose technologies have provided solutions and applications to a wide variety of complex biomedical and healthcare problems. The purposes of this review are to present a comprehensive analysis of past and recent biomedical research findings and developments of electronic-nose sensor technologies, and to identify current and future potential e-nose applications that will continue to advance the effectiveness and efficiency of biomedical treatments and healthcare services for many years. An abundance of electronic-nose applications has been developed for a variety of healthcare sectors including diagnostics, immunology, pathology, patient recovery, pharmacology, physical therapy, physiology, preventative medicine, remote healthcare, and wound and graft healing. Specific biomedical e-nose applications range from uses in biochemical testing, blood-compatibility evaluations, disease diagnoses, and drug delivery to monitoring of metabolic levels, organ dysfunctions, and patient conditions through telemedicine. This paper summarizes the major electronic-nose technologies developed for healthcare and biomedical applications since the late 1980s when electronic aroma detection technologies were first recognized to be potentially useful in providing effective solutions to problems in the healthcare industry