Chemical Lab. S. side

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981.

Chem. Lab. [Chemical Laboratory]

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981.

Chemical Laboratory on Campus

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981. Image taken from northwest corner of addition of 1890. Duplicate of BL004177.

Chemical Laboratory

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981. Duplicate of BL004177.On verso: Before 1910.

Chemical Laboratory

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981. On verso: Now Pharmacology and Economics as of 1950. To the left of the Diag in front of Gen'l Library.

Technical methods of chemical analysis,

"A revised edition of Dr. F. Böckmann̓s Chemisch-technische Untersuchungsmethoden, edited by Professor G. Lunge, was published in 1899 ... practically a new work ... adapted to modern methods of work. In 1904 a second edition was called for, in which the whole of the subject matter was thoroughly revised and brought up to date ... The English translation has been made from the second German edition ... A bibliography ... is appended to each section, and all important tables, in addition to having printed in the text, are also printed for reference at the end of each volume."-Pref.

Chemical Laboratory

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981. On verso: Old Chemical Laboratory. University of Michigan. Where I spent two very profitable years, 1891-1893. George Wagner.

Chemical Building

Built in 1856. First chemical laboratory at a state university. Building served medical students and others as both laboratory and classroom. Situated just west and south of the original medical building. Additions made to the one-story building in 1861, 1866, 1868, 1874. In 1880 a two-story addition was added with subsequent additions in 1889 and 1901. Became Economics Building in 1908. Pharmacology occupied north wing 1908-1981. Destroyed by fire Christmas Eve 1981. This image is from the northwest. Male person seated by tree.

Binomial leap methods for simulating stochastic chemical kinetics

This paper discusses efficient simulation methods for stochastic chemical kinetics. Based on the tau-leap and midpoint tau-leap methods of Gillespie [D. T. Gillespie, J. Chem. Phys. 115, 1716 (2001)], binomial random variables are used in these leap methods rather than Poisson random variables. The motivation for this approach is to improve the efficiency of the Poisson leap methods by using larger stepsizes. Unlike Poisson random variables whose range of sample values is from zero to infinity, binomial random variables have a finite range of sample values. This probabilistic property has been used to restrict possible reaction numbers and to avoid negative molecular numbers in stochastic simulations when larger stepsize is used. In this approach a binomial random variable is defined for a single reaction channel in order to keep the reaction number of this channel below the numbers of molecules that undergo this reaction channel. A sampling technique is also designed for the total reaction number of a reactant species that undergoes two or more reaction channels. Samples for the total reaction number are not greater than the molecular number of this species. In addition, probability properties of the binomial random variables provide stepsize conditions for restricting reaction numbers in a chosen time interval. These stepsize conditions are important properties of robust leap control strategies. Numerical results indicate that the proposed binomial leap methods can be applied to a wide range of chemical reaction systems with very good accuracy and significant improvement on efficiency over existing approaches. (C) 2004 American Institute of Physics.

A multi-scaled approach for simulating chemical reaction systems

In this paper we give an overview of some very recent work, as well as presenting a new approach, on the stochastic simulation of multi-scaled systems involving chemical reactions. In many biological systems (such as genetic regulation and cellular dynamics) there is a mix between small numbers of key regulatory proteins, and medium and large numbers of molecules. In addition, it is important to be able to follow the trajectories of individual molecules by taking proper account of the randomness inherent in such a system. We describe different types of simulation techniques (including the stochastic simulation algorithm, Poisson Runge–Kutta methods and the balanced Euler method) for treating simulations in the three different reaction regimes: slow, medium and fast. We then review some recent techniques on the treatment of coupled slow and fast reactions for stochastic chemical kinetics and present a new approach which couples the three regimes mentioned above. We then apply this approach to a biologically inspired problem involving the expression and activity of LacZ and LacY proteins in E. coli, and conclude with a discussion on the significance of this work.

Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot

The cyclotides constitute a recently discovered family of plant-derived peptides that have the unusual features of a head-to-tail cyclized backbone and a cystine knot core. These features are thought to contribute to their exceptional stability, as qualitatively observed during experiments aimed at sequencing and characterizing early members of the family. However, to date there has been no quantitative study of the thermal, chemical, or enzymatic stability of the cyclotides. In this study, we demonstrate the stability of the prototypic cyclotide kalata B1 to the chaotropic agents 6 M guanidine hydrochloride (GdHCl) and 8 M urea, to temperatures approaching boiling, to acid, and following incubation with a range of proteases, conditions under which most proteins readily unfold. NMR spectroscopy was used to demonstrate the thermal stability, while fluorescence and circular dichroism were used to monitor the chemical stability. Several variants of kalata B1 were also examined, including kalata 132, which has five amino acid substitutions from B1, two acyclic permutants in which the backbone was broken but the cystine knot was retained, and a two-disulfide bond mutant. Together, these allowed determinations of the relative roles of the cystine knot and the circular backbone on the stability of the cyclotides. Addition of a denaturant to kalata B1 or an acyclic permutant did not cause unfolding, but the two-disulfide derivative was less stable, despite having a similar three-dimensional structure. It appears that the cystine knot is more important than the circular backbone in the chemical stability of the cyclotides. Furthermore, the cystine knot of the cyclotides is more stable than those in similar-sized molecules, judging by a comparison with the conotoxin PVIIA. There was no evidence for enzymatic digestion of native kalata B1 as monitored by LC-MS, but the reduced form was susceptible to proteolysis by trypsin, endoproteinase Glu-C, and thermolysin. Fluorescence spectra of kalata B1 in the presence of dithiothreitol, a reducing agent, showed a marked increase in intensity thought to be due to removal of the quenching effect on the Trp residue by the neighboring Cys5-Cys17 disulfide bond. In general, the reduced peptides were significantly more susceptible to chemical or enzymatic breakdown than the oxidized species.

Chemical characterization of earth's most ancient clastic metasediments from the Isua Greenstone Belt, southern West Greenland

New and published major and trace element abundances of elastic metasediments (mainly garnet-biotite-plagioclase schists) from the similar to 3.8 Ga Isua Greenstone Belt (IGB), southern West Greenland, are used in an attempt to identify the compositional characteristics of the protoliths of these sediments. Compositionally, the metasediments are heterogeneous with enrichment of LREE (La/Sm-chord = 1.1-3.9) and variable enrichment and depletion of HREE (Gd/Yb-chord = 0.8-4.3). Chondrite-normalized Eu is also variable, spanning a range from relative Eu depletion to enrichment (Eu/Eu* = 0.6-1.3). A series of geochemical and geological criteria provides conclusive evidence for a sedimentary origin, in disagreement with some previous studies that questioned the presence of genuine elastic metasediments. In particular, trace element systematics of IGB metasediments show strong resemblance to other well-documented Archaean clastic sediments, and are consistent with a provenance consisting of ultramafic, malic and felsic igneous rocks. Two schists, identified as metasomatized mafic igneous rocks from petrographic and field evidence, show distinct compositional differences to the metasediments. Major element systematics document incipient-to-moderate source weathering in the majority of metasediments, while signs of secondary K-addition are rare. Detailed inspection of Eu/Eu*, Fe2O3 and CIW (chemical index of weathering) relationships reveals that elevated iron contents (when compared to averages for continental crust) and strong relative enrichment in Eu may be due to precipitation of marine Fe-oxyhydroxides during deposition or diagenesis on the seafloor. Some of the IGB metasediments have yielded anomalous Nd-142 and W-182 isotopic compositions that were respectively interpreted in terms of early mantle differentiation processes and the presence of a meteorite component. Alternatively, W and possibly Nd isotopes could have been affected by thermal neutron capture on the Hadean surface. The latter process was tested in this study by analysis of Sm isotope compositions, which serve as an effective monitor for neutron capture effects. As no anomalous variation from terrestrial values was detected, we infer that isotope systematics (including W-182 and Nd-142) of IGB metasediments were not affected by neutron capture, but reflect decay of radioactive parent isotopes. Copyright (c) 2005 Elsevier Ltd.

Synthesis and characterization of turbostratic carbons prepared by catalytic chemical vapour decomposition of acetylene

The turbostratic mesoporous carbon blacks were prepared by catalytic chemical vapour decomposition (CCVD) of acetylene using Ni/MgO catalysts prepared by co-precipitation. The relationship between deposition conditions and the nanostructures of resultant carbon black materials was investigated. It was found that the turbostratic and textural structures of carbon blacks are dependent on the deposition temperature and nickel catalyst loading. Higher deposition temperature increases the carbon crystallite unit volume V-nano and reduces the surface area of carbon samples. Moreover, a smaller V-nano is produced by a higher Ni loading at the same deposition temperature. In addition of the pore structure and the active metal surface area of the catalyst, the graphitic degree or electronic conductivity of the carbon support is also a key issue to the activity of the supported catalyst. V-nano is a very useful parameter to describe the effect of the crystalline structure of carbon blacks on the reactivity of carbon blacks in oxygen-carbon reaction and the catalytic activity of carbon-supported catalyst in ammonia decomposition semi-quantitatively. (C) 2006 Elsevier B.V. All rights reserved.

Human sulfotransferases and their role in chemical metabolism

Sulfonation is an important reaction in the metabolism of numerous xenobiotics, drugs, and endogenous compounds. A supergene family of enzymes called sulfotransferases (SULTs) catalyze this reaction. In most cases, the addition of a sulfonate moiety to a compound increases its water solubility and decreases its biological activity. However, many of these enzymes are also capable of bioactivating procarcinogens to reactive electrophiles. In humans three SULT families, SULT1, SULT2, and SULT4, have been identified that contain at least thirteen distinct members. SULTs have a wide tissue distribution and act as a major detoxification enzyme system in adult and the developing human fetus. Nine crystal structures of human cytosolic SULTs have now been determined, and together with site-directed mutagenesis experiments and molecular modeling, we are now beginning to understand the factors that govern distinct but overlapping substrate specificities. These studies have also provided insight into the enzyme kinetics and inhibition characteristics of these enzymes. The regulation of human SULTs remains as one of the least explored areas of research in the field, though there have been some recent advances on the molecular transcription mechanism controlling the individual SULT promoters. Interindividual variation in sulfonation capacity may be important in determining an individual's response to xenobiotics, and recent studies have begun to suggest roles for SULT polymorphism in disease susceptibility. This review aims to provide a summary of our present understanding of the function of human cytosolic sulfotransferases.

Phytotoxicity of surface waters of the Thames and Brisbane River Estuaries: A combined chemical analysis and bioassay approach for the comparison of two systems

The Thames Estuary, UK, and the Brisbane River, Australia, are comparable in size and catchment area. Both are representative of the large and growing number of the world's estuaries associated with major cities. Principle differences between the two systems relate to climate and human population pressures. In order to assess the potential phytotoxic impact of herbicide residues in the estuaries, surface waters were analysed with a PAM fluorometry-based bioassay that employs the photosynthetic efficiency (photosystem II quantum yield) of laboratory cultured microalgae, as an endpoint measure of phytotoxicity. In addition, surface waters were chemically analysed for a limited number of herbicides. Diuron atrazine and simazine were detected in both systems at comparable concentrations. In contrast, bioassay results revealed that whilst detected herbicides accounted for the observed phytotoxicity of Brisbane River extracts with great accuracy, they consistently explained only around 50% of the phytotoxicity induced by Thames Estuary extracts. Unaccounted for phytotoxicity in Thames surface waters is indicative of unidentified phytotoxins. The greatest phytotoxic response was measured at Charing Cross, Thames Estuary, and corresponded to a diuron equivalent concentration of 180 ng L-1. The study employs relative potencies (REP) of PSII impacting herbicides and demonstrates that chemical analysis alone is prone to omission of valuable information. Results of the study provide support for the incorporation of bioassays into routine monitoring programs where bioassay data may be used to predict and verify chemical contamination data, alert to unidentified compounds and provide the user with information regarding cumulative toxicity of complex mixtures. (c) 2005 Elsevier B.V. All rights reserved.