Single- and few-walled carbon nanotubes grown at temperatures as low as 450 degrees c: electrical and field emission characterization.

Single-wall (SW-) and few-walled (FW-) carbon nanotubes (CNTs) were synthesized on aluminum/ cobalt coated silicon at temperatures as low as 450 degrees C by plasma enhanced chemical vapor deposition technique (PECVD). The SWCNTs and FWCNTs grow vertically oriented and well separated from each other. The cold field emission studies of as-grown SWCNTs and FWCNTs showed low turn-on field emission threshold voltages, strongly dependent of the nanotubes morphology. Current-voltage curves of individual CNTs, measured by conductive atomic force microscopy (CAFM), showed an electrical resistance of about 90 Komega, that is attributed mainly to the resistance of the contact between the CNTs and the conductive CAFM tip (Au and Pt).

Macrophage esterase: identification, purification and properties of a chymotrypsin-like esterase from lung that hydrolyses and transfers nonpolar amino acid esters.

A chymotrypsin-like esterase was purified from beef lung. This lysosomal enzyme, not previously characterized, seemed to be composed of two or more forms with molecular weights of about 52 000. It hydrolysed N-benzoyl-DL-phenylalanine beta-naphthol ester at acid and neutral pH; it polymerized L-phenylalanine methyl ester(Phe-OMe) at neutral pH; and it transferred the Phe-residue from Phe-OMe to hydroxylamine at neutral pH. Phenylmethanesulfonyl fluoride, an inhibitor of hydrolytic enzymes with serine in their catalytic site, inhibited this enzyme, but pepstatin, the cathepsin D (EC 3.4.4.23) inhibitor, did not. Sulfhydryl reagents were not required for activity. Macrophages, especially pulmonary alveolar macrophages, were a rich source of this esterase, so it is likely that the enzyme purified from lung came from its macrophages. The esterase hydrolysed and transferred monoamino acid esters, especially those of the aromatic type. Cathepsin C, the dipeptidyl peptide hydrolase (EC 3.4.14.1), acted only on dipeptide esters and amides. Pancreatic chymotrypsin acted on both monoamino acid and dipeptide esters. The chymotrypsin-like esterase did not hydrolyse hemoglobin, casein, or plasma albumin. Thus its proteolytic activity, if present, must be limited to specific substrates, as yet unknown.

Oriented carbon nanostructures containing nitrogen obtained by ion beam assisted deposition.

In this paper, we report the deposition of graphite multilayer containing nitrogen covering nanometric nickel particles. In-situ photoelectron emission spectroscopy (XPS) reveals the presence of nitrogen in the carbon layer covering the nickel particles. The field emission properties of the structures are reported. Atomic force microscopy displays regular domelike structures. Raman spectroscopy shows the characteristic frequencies associated with graphite and disordered structures. High-resolution transmission electron microscopy confirms the presence of multiwall well-organized graphite layers covering the nickel particles. Disorder increases on increasing nitrogen content. The samples were prepared in-situ by depositing first a few atomic layers of nickel and subsequent islands formation by thermal annealing. Then, an argon ion beam bombards an ultrapure carbon target and simultaneously the growing film is assisted with a second low-energy nitrogen ion beam (ion beam assisted deposition).