Two-band superconductivity in LaFeAsO0.89F0.11 at very high magnetic fields.

The recent synthesis of the superconductor LaFeAsO(0.89)F(0.11) with transition temperature T(c) approximately 26 K (refs 1-4) has been quickly followed by reports of even higher transition temperatures in related compounds: 41 K in CeFeAsO(0.84)F(0.16) (ref. 5), 43 K in SmFeAsO(0.9)F(0.1) (ref. 6), and 52 K in NdFeAsO(0.89)F(0.11) and PrFeAsO(0.89)F(0.11) (refs 7, 8). These discoveries have generated much interest in the mechanisms and manifestations of unconventional superconductivity in the family of doped quaternary layered oxypnictides LnOTMPn (Ln: La, Pr, Ce, Sm; TM: Mn, Fe, Co, Ni; Pn: P, As), because many features of these materials set them apart from other known superconductors. Here we report resistance measurements of LaFeAsO(0.89)F(0.11) at high magnetic fields, up to 45 T, that show a remarkable enhancement of the upper critical field B(c2) compared to values expected from the slopes dB(c2)/dT approximately 2 T K(-1) near T(c), particularly at low temperatures where the deduced B(c2)(0) approximately 63-65 T exceeds the paramagnetic limit. We argue that oxypnictides represent a new class of high-field superconductors with B(c2) values surpassing those of Nb(3)Sn, MgB(2) and the Chevrel phases, and perhaps exceeding the 100 T magnetic field benchmark of the high-T(c) copper oxides.

Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides.

The distribution of beta 1,2 N-acetylglucosaminyltransferase I (NAGT I), alpha 1,3-1,6 mannosidase II (Mann II), beta 1,4 galactosyltransferase (GalT), alpha 2,6 sialyltransferase (SialylT) was determined by immuno-labelling of cryo-sections from HeLa cell lines. Antibody labelling in the HeLa cell line was made possible by stable expression of epitope-tagged forms of these proteins or forms from species to which specific antibodies were available. NAGT I and Mann II had the same distribution occupying the medial and trans cisternae of the stack. GalT and SialylT also had the same distribution but they occupied the trans cisterna and the trans-Golgi network (TGN). These results generalise our earlier observations on the overlapping distribution of Golgi enzymes and show that each of the trans compartments of the Golgi apparatus in HeLa cells contains unique mixtures of those Golgi enzymes involved in the construction of complex, N-linked oligosaccharides.

Kin recognition between medial Golgi enzymes in HeLa cells.

The medial Golgi enzymes, N-acetylglucosaminyltransferase I (NAGT I) and mannosidase II (Mann II), and the trans Golgi enzyme, beta-1,4-galactosyltransferase (GalT) were each retained in the endoplasmic reticulum (ER) by grafting on the cytoplasmic tail of the p33 invariant chain. Transient and stable expression of p33/NAGT I in HeLa cells caused relocation of endogenous Mann II to the ER and transient expression of p33/Mann II had a similar effect on endogenous NAGT I. Neither of these endogenous medial enzymes were affected by transient expression of p33/GalT. These data provide strong evidence for kin recognition between medial Golgi enzymes and suggest a role for them in the organization of the Golgi stack.