We report the atomic structure of a multicomponent Cu45Zr45Ag10 bulk metallic glass investigated by state-of-the-art experimental and computational techniques. In comparison with a binary Cu50Zr50 metallic glass, Zr-rich interpenetrating clusters centered by paired and stringed Ag atoms and Cu-rich icosahedra are widely observed in the ternary Cu45Zr45Ag10 alloy. The atomic-scale heterogeneity caused by chemical short- and medium-range order is found to play a key role in stabilizing the liquid phase and in improving the glass forming ability of the multicomponent alloy.

Ganglioside-hydrolyzing sialidase activity was solubilized from rat brain particulate fraction by using Triton X-100 plus sodium deoxycholate. When chromatographed on AH-Sepharose 4B, the solubilized activity was resolved into two peaks, which were designated sialidases I and II in order of elution. The two sialidases were purified by using sequential chromatographies on Octyl-Sepharose CL-4B, Phenyl-Sepharose CL-4B, and Sephadex G-200. Sialidase II was purified further by Mono Q-FPLC. Overall purification was 450- and 2,150-fold, for sialidases I and II, respectively. Purified sialidases I and II were maximally active at near pH 5.0 and exhibited M = 70,000 by gel filtration. Sialidase I hydrolyzed gangliosides but scarcely other substrates including 4-methylumbelliferyl-NeuAc (4MU-NeuAc). Sialidase II hydrolyzed oligosaccharides, glycoproteins, and 4MU-NeuAc although gangliosides appeared to be preferential substrates. Sialidase II cleaved GM2 much faster than sialidase I. An antibody raised in rabbits against sialidase I reacted with only sialidase I and an antibody against sialidase II reacted with only sialidase II. A subcellular distribution study suggested sialidase I in the synaptosomal membrane and sialidase II in the synaptosomal and lysosomal membranes, and this was verified by using the above antibodies.

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Cytosolic sialidase was purified from rat skeletal muscle, and the purified enzyme migrated as a single band of Mr 43,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A polyclonal antibody raised against the enzyme inhibited and immunoprecipitated rat liver cytosolic sialidase as well as the muscle enzyme but failed to cross-react with the intralysosomal sialidase of rat liver and membrane sialidases I (synaptosomal) and II (lysosomal) of rat brain. The antibody against brain membrane sialidase I (anti-I) and that against sialidase II (anti-II), which could be useful to discriminate the two enzymes, did not cross-react with the intralysosomal and cytosolic sialidases of liver. Although more than 90% of liver plasma membrane sialidase was immunoprecipitated with anti-I, only 60% of liver lysosomal membrane sialidase was immunoprecipitated with anti-II, the remainder being immunoprecipitated with anti-I. In confirmation of these data, liver lysosomal membrane exhibited two peaks of ganglioside sialidase corresponding to the membrane sialidases I and II on Aminohexyl-Sepharose chromatography while only one peak of ganglioside sialidase corresponding to sialidase I was observed for liver plasma membrane. These results indicate that the four types of rat sialidase are proteins distinct from one another and that the three kinds of antisera described above are useful for discriminating these sialidases qualitatively and probably quantitatively.

The microstructure of a melt-quenched Mg 98 Cu 1 Y 1 alloy has been studied by high-resolution transmission electron microscopy (HRTEM) and high-angle annular detector dark-field scanning transmission electron microscopy (HAADF-STEM). We have found Cu-and Y-rich precipitates, which are uniformly dispersed in Mg-matrix grains. The precipitates are aligned parallel to the c-plane of the Mg-matrix crystal, and have the peculiar morphology consisting of a disk-shaped amorphous core sandwiched between 14H-typed long period stacking order (LPSO) crystals. A relatively stable supper-cooled liquid phase in an Mg-Cu-Y alloy system, and the formation and growth of the LPSO crystals from the amorphous phase are responsible for the peculiar morphology of the precipitates.

Magnetic and crystallographic measurements have been made for the compounds RCo4M (R = Y, Nd, and Ho; M = B, Al, and Ga) to intercompare the magnetic properties of RCOJB, RCoaM (M = Al and Ga) and RCo5. The compounds RCo4B crystallize in the CeCo,B type structure, while RCo4M (M = Al and Ga) in the CaCuS type. The following main conclusions have been obtained: ( 1) the Curie temperature and the averaged Co-moment of RCo,M (R = Y, Nd, and Ho; M = B, Al, and Ga) are lower and smaller than those of RCo5, respectively, and 6i-site Co-moment in RCo$ is smaller than the 2csite Co-moment by the influence of the neighboring B-layer; (2) magnetocrystalline anisotropy of R-sublattice of RCo4B is stronger than that of RCo,, while that of RCo4A1 is remarkably weaker than that of RCo,; (3) the Co-sublattice anisotropy constants of YCo&I (M = B and Al) are 20% or less of that of YCo,; and (4) JR-o0 and Jco-cO, which are the exchange parameters of the atomic pairs in NdCo,+M (M = B and Al), have been estimated to be JR.&k N 7 K and Jc,.co/k N 200 K, where k is the Boltzman constant. 5551

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The effects of surfactant apoprotein A (SP-A) on the superoxide production of rat alveolar macrophages (AM) were studied. Superoxide production was measured by the ferricytochrome c reduction method. When AM were incubated with SP-A only during the measurement of superoxide production, superoxide production was not influenced by SP-A. However, when AM were preincubated with SP-A at a concentration of 1, 2, and 10 micrograms/ml, superoxide production by AM was significantly inhibited (P < 0.05, P < 0.01, P < 0.01, respectively). The superoxide production of AM stimulated by PMA was significantly inhibited by SP-A at a concentration of 1 microgram/ml (P < 0.01), and superoxide production stimulated by zymosan was also inhibited by SP-A at a concentration of 10 micrograms/ml (P < 0.05). Suppression of superoxide production of unstimulated and PMA-stimulated AM was significantly inhibited by anti-SP-A antibody. Superoxide generation by the xanthine and xanthine oxidase system was not affected by the presence of SP-A. Our results suggest that superoxide production of AM can be inhibited by SP-A and that this inhibitory effect on AM is due to a specific effect of SP-A. From these results, it is speculated that SP-A may have a protective role for oxidant injury by AM in the lung.