Oxidation of glucose by iodine in the presence of insulin

This investigation was undertaken with the purpose of determining whether insulin, alone or in the presence of certain animal fluids, has any influence upon glucose in vitro. The establishment of such an influence might have much significance in relation both to the study of carbohydrate metabolism and to the development of methods of assaying insulin

Inhibitor specificity of amine oxidase

Although at the present time it appears clear that amine oxidase oxidation of adrenalin, or other o-diphenolic pressor amines such as were studied by Richter (6), does not play a significant physiological role, it is equally clear that the inactivation of aliphatic amines, phenethylamine and probably 4-hydroxyphenethylamine (tyramine), does predominantly take place by amine oxidase oxidation. In view of the evidence from the experiments of Ewins and Laidlaw (8) and a later study by Guggenheim and Löffler (9), such amine oxidations chiefly occur in the liver. In the present studies, an attempt was made to value quantitatively the inhibition of some of these particular type compounds by certain types of amines which are not themselves oxidized by the enzyme system (see Alles and Heegaard (10))

Substrate specificity of amine oxidase

The tyramine oxidase activity of liver extracts found by Hare (1), the aliphatic amine oxidase activity of brain, kidney, and liver extracts observed by Pugh and Quastel (2), and the adrenalin oxidase activity of similar extracts noted by Blaschko, Richter, and Schlossman (3) were brought under a common enzyme view-point by the latter authors. They were able to show (4) that extracts of brain, instestine, kindey, and liver from a number of mammals or representatives of the birds, reptiles, amphibians, and fishes all acted to absorb oxygen in the presence of several amine substrates. Hare (1) had shown that tyramine and phenethylamine form ammonia in the course of such oxidations, and Richter (5) showed that an ethylamino and a dimethylamino compound, as well as a number of methylamino and amino compounds, all yield the corresponding alkyl-amines or ammonia in the enzymic oxidation. The conslusion that the demonstrated variey of such enzymic activity can be acribed to the presence of a single type pf amine oxidase was dependent in large part on observations that the relative activities of a preparation from one source on a series of substrates bear some relation to the relative activities exhibited by a preparation from another source. Further evidence depended on the action of certain amines as inihibitors and apparent competition between substrates when two oxidizable substrates are present in the system. The degree to which relative activities of different enzyme preparations were constant in a series of substrates was not good in the data reported, and the fact that Hare (1) had not been able to note activity of the liver preparations she used upon adrenalin as the substrate appeared to require special explanations

Tyrosinase and phenolic pressor amines

Basic to the consideration of the action of tyrosinase on the oxidation of phenolic pressor amines are the observations of Keilin and Mann (16) and of Nelson and his coworkers (17-19) that show that different preparations may vary considerably in their relative actions on monophenols and o-diphenols. Both of these types of activity appear to belong to the same enzyme complex, as they bear a proportionality to the same copper content. However, since the activities vary with the purity and method of purification, each enzyme preparation must be defined in terms of both monophenolase and o-diphenolase activities. This was done in the present studies, and modifications of previously described preparative methods were required to retain a reasonable proportioning of such activities in purified preparations

Comparison of Fabrication Methods for Fiber‐Optic Ultrasound Transmitters Using Candle‐Soot Nanoparticles

Candle-soot nanoparticles (CSNPs) have shown great promise for fabricating optical ultrasound (OpUS) transmitters. They have a facile, inexpensive synthesis whilst their unique, porous structure enables a fast heat diffusion rate which aids high-frequency ultrasound generation necessary for high-resolution clinical imaging. These composites have demonstrated high ultrasound generation performance showing clinically relevant detail, when applied as macroscale OpUS transmitters comprising both concave and planar surfaces, however, less research has been invested into the translation of this material's technology to fabricate fiber-optic transmitters for image guidance of minimally invasive interventions. Here, are reported two fabrication methods of nanocomposites composed of CSNPs embedded within polydimethylsiloxane (PDMS) deposited onto fiber-optic end-faces using two different optimized fabrication methods: “All-in-One” and “Direct Deposition.” Both types of nanocomposite exhibit a smooth, black domed structure with a maximum dome thickness of 50 µm, broadband optical absorption (>98% between 500 and 1400 nm) and both nanocomposites generated high peak-to-peak ultrasound pressures (>3 MPa) and wide bandwidths (>29 MHz). Further, high-resolution (<40 µm axial resolution) B-mode ultrasound imaging of ex vivo lamb brain tissue demonstrating how CSNP-PDMS OpUS transmitters can allow for high fidelity minimally invasive imaging of biological tissues is demonstrated