Calibration of a fission gas monitor

Calibration of argon gas neutron activation sampling devic

Manufacturing checkout of orbital operational stages Midterm report, period ending 24 Feb. 1965

Manufacturing checkout of orbital operational Saturn S-IVB stage and instrument unit for parking orbit operation

Predicting inheritance of breeding herds

How much of their advantage for a particular trait do superior animals transmit to their offspring? Heritability estimates help us answer this important question. This guide explains the meaning of heritability estimates, how they are calculated, and how they may be used for the improvement of livestock through breeding.John W. Massey, John F. Lasley, and Billy N. Day (Department of Animal Husbandry, College of Agriculture)Revised 7/80/8

Nonenzymatically Glucosylated Albumin: In Vitro Preparation and Isolation from Normal Human Serum

Incubation of human serum with D-[6-3H]glucose resulted in the gradual accumulation of radioactivity in acid-precipitable material. Upon chromatography on Sephadex G-200, radioactivity was found associated with each of the major molecular weight classes of serum protein. Purified human serum albumin was also glucosylated in vitro upon exposure to D-[6-3H]glucose in phosphate-buffered saline. The glucosylated and unmodified albumins were separated by ion exchange chromatography. The physiological significance of these observations in vitro was confirmed by the isolation and quantitation of glucosylated albumin from normal human serum. Glucosylated albumin represents approximately 6 to 15% of total serum albumin in normal adults. The post-translational modification appears to occur by a nonenzymatic process analogous to that responsible for glucosylation of hemoglobin A to hemoglobin AIc, i.e. through Schiff base formation and Amadori rearrangement to a ketoamine derivative

IT-technology in the budgeting

Budgeting plays an important role in modern organization, it is the tool that is necessary for the survival of the company in a competitive environment. Budgeting has become necessary business management process, and like any management activities, it requires automation

Nonenzymatic Glucosylation of Rat Albumin: Studies in Vitro and in Vivo

Incubation of rat serum with D-glucose in vitro resulted in nonenzymatic glucosylation of serum proteins. Analysis of freshly isolated rat albumin by ion exchange chromatography indicated that the glucosylated albumin accounts for 6.7.+-. 0.9% of total albumin in normal rat serum. Glucosylation of rat albumin in vitro was 1st order with respect to glucose and albumin concentrations and occurs primarily (\u3e 90%) at intrachain lysine residues. Kinetic analysis and inhibition of glucosylation by aspirin suggest that 1 reactive lysine residue is the primary site of glucosylation. Less than 5% of the radioactivity from glucosyl-albumin was released as glucose or mannose by hydrolysis conditions normally used for the analysis of neutral sugars in glycoproteins. Studies in vivo demonstrated that the half-life of albumin in normal rats was unaffected by the addition of 1 mol of glucose/mol of albumin. In addition, glucosylation was a stable modification since 125i-albumin isolated up to 3 days after injection of glucosylated 125i-albumin was recovered only in the glucosylated fraction. In contrast, following injection of unglucosylated 125i-albumin there was a gradual shift of 125i radioactivity to the glucosylated albumin fraction, as would be predicted for nonenzymatic glucosylation occurring in the circulation. Finally, levels of glucosylated albumin isolated from diabetic rats (alloxan induced) were significantly (4-fold) elevated 4 days after withdrawal from insulin therapy. The rat should be a suitable animal model for in vivo studies on nonenzymatic glucosylation of albumin and other serum proteins in normal and diabetic metabolic states

Branching Transition of a Directed Polymer in Random Medium

A directed polymer is allowed to branch, with configurations determined by global energy optimization and disorder. A finite size scaling analysis in 2D shows that, if disorder makes branching more and more favorable, a critical transition occurs from the linear scaling regime first studied by Huse and Henley [Phys. Rev. Lett. 54, 2708 (1985)] to a fully branched, compact one. At criticality clear evidence is obtained that the polymer branches at all scales with dimension ${\bar d}_c$ and roughness exponent $\zeta_c$ satisfying $({\bar d}_c-1)/\zeta_c = 0.13\pm 0.01$, and energy fluctuation exponent $\omega_c=0.26 \pm0.02$, in terms of longitudinal distanceComment: REVTEX, 4 pages, 3 encapsulated eps figure

Modeling Exposure-Lag-Response Associations with Penalized Piece-wise Exponential Models

We present a novel approach for the flexible modeling of exposure-lag-response associations, i.e., time-to-event data where multiple past exposures are cumulatively associated with the hazard after a certain temporal delay. Our method is based on piece-wise exponential models and allows estimation of a wide variety of effects, including potentially smooth and time-varying effects as well as cumulative effects with leads and lags, taking advantage of the advanced inference methods that have recently been developed for generalized additive mixed models

Reaction Landscape of a Pentadentate N5-Ligated MnII Complex with O2•− and H2O2 Includes Conversion of a Peroxomanganese(III) Adduct to a Bis(μ-oxo)dimanganese(III,IV) Species

Herein we describe the chemical reactivity of the mononuclear [MnII(N4py)(OTf)](OTf) (1) complex with hydrogen peroxide and superoxide. Treatment of 1 with one equivalent superoxide at −40 °C in MeCN formed the peroxomanganese(III) adduct, [MnIII(O2)(N4py)]+ (2) in ~30% yield. Complex 2 decayed over time and the formation of the bis(μ-oxo)dimanganese(III,IV) complex, [MnIIIMnIV(μ-O)2(N4py)2]3+ (3) was observed. When 2 was formed in higher yields (~60%) using excess superoxide, the [MnIII(O2)(N4py)]+ species thermally decayed to MnII species and 3 was formed in no greater than 10% yield. Treatment of [MnIII(O2)(N4py)]+ with 1 resulted in the formation of 3 in ~90% yield, relative to the concentration of [MnIII(O2)(N4py)]+. This reaction mimics the observed chemistry of Mn-ribonucleotide reductase, as it features the conversion of two MnII species to an oxo-bridged MnIIIMnIV compound using O2− as oxidant. Complex 3 was independently prepared through treatment of 1 with H2O2 and base at −40 °C. The geometric and electronic structures of 3 were probed using electronic absorption, electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), variable-temperature, variable-field MCD (VTVH-MCD), and X-ray absorption (XAS) spectroscopies. Complex 3 was structurally characterized by X-ray diffraction (XRD), which revealed the N4py ligand bound in an unusual tetradentate fashion