THE DESIGN AND ANALYSIS OF EXPERIMENTS. By Oscar Kempthorne. New York, John Wiley and Sons, Inc., 1952. 631 pp. $8.50. This book by a teacher of statistics (as well as a consultant for \"experimenters\") is a comprehensive study of the philosophical background for the statistical design of experiment. It is necessary to have some facility with algebraic notation and manipulation to be able to use the volume intelligently. The problems are presented from the theoretical point of view, without such practical examples as would be helpful for those not acquainted with mathematics. The mathematical justification for the techniques is given. As a somewhat advanced treatment of the design and analysis of experiments, this volume will be interesting and helpful for many who approach statistics theoretically as well as practically. With emphasis on the \"why,\" and with description given broadly, the author relates the subject matter to the general theory of statistics and to the general problem of experimental inference. MARGARET J. ROBERTSON

The Design and Analysis of Experiments

KEGG(Kyoto Encyclopedia of Genes and Genomes)〔和文〕 (特集 ゲノム医学の現在と未来--基礎と臨床) -- (データベース)

I read this book the same weekend that the Packers took on the Rams, and the experience of the latter event, obviously, colored my judgment. Although I abhor anything that smacks of being a handbook (like, \"How to Earn a Merit Badge in Neurosurgery\") because too many volumes in biomedical science already evince a boyscout-like approach, I must confess that parts of this volume are fast, scholarly, and significant, with certain reservations. I like parts of this well-illustrated book because Dr. Sj6strand, without so stating, develops certain subjects on technique in relation to the acquisition of judgment and sophistication. And this is important! So, given that the author (like all of us) is somewhat deficient in some areas, and biased in others, the book is still valuable if the uninitiated reader swallows it in a general fashion, realizing full well that what will be required from the reader is a modulation to fit his vision, propreception, adaptation and response, and the kind of problem he is undertaking. A major deficiency of this book is revealed by comparison of its use of physics and of chemistry to provide understanding and background for the application of high resolution electron microscopy to problems in biology. Since the volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of The instrument and its ancillary tools are simply and well presented. The potential use of chemical or cytochemical information as it relates to biological fine structure , however, is quite deficient. I wonder when even sophisticated morphol-ogists will consider fixation a reaction and not a technique; only then will the fundamentals become self-evident and predictable and this sine qua flon will become less mystical. Staining reactions (the most inadequate chapter) ought to be something more than a technique to selectively enhance contrast of morphological elements; it ought to give the structural addresses of some of the chemical residents of cell components. Is it pertinent that auto-radiography gets singled out for more complete coverage than other significant aspects of cytochemistry by a high resolution microscopist, when it has a built-in minimal error of 1,000 A in standard practice? I don't mean to blind-side (in strict football terminology) Dr. Sj6strand's efforts for what is \"routinely used in our laboratory\"; what is done is usually well done. It's just that …

Methods in Enzymology.

Extracellular enzymes mediate the degradation, transformation and mineralization of soil organic matter. The activity of cellulases, phosphatases and other hydrolases has received extensive study and in many cases stoichiometric relationships and responses to disturbances are well established. In contrast, phenol oxidase and peroxidase activities, which are often uncorrelated with hydrolase activities, have been measured in only a small subset of soil enzyme studies. These enzymes are expressed for a variety of purposes including ontogeny, defense and the acquisition of carbon and nitrogen. Through excretion or lysis, these enzymes enter the environment where their aggegrate activity mediates key ecosystem functions of lignin degradation, humification, carbon mineralization and dissolved organic carbon export. Phenol oxidases and peroxidases are less stable in the environment than extracellular hydrolases, especially when associated with organic particles. Activities are also affected, positively and negatively, by interaction with mineral surfaces. High spatiotemporal variation obscures their relationships with environmental variables and ecological process. Across ecosystems, phenol oxidase and peroxidase activities generally increase with soil pH, a finding not predicted from the pH optima of purified enzymes. Activities associated with plant litter and particulate organic matter often correlate with decomposition rates and potential activities generally increase with the lignin and secondary compound content of the material. At the ecosystem scale, nitrogen amendment alters the expression of phenol oxidase and peroxidase enzymes more broadly than culture studies imply and these responses correlate with positive and negative changes in litter decomposition rates and soil organic matter content. At the global scale, N amendment of basidiomycete-dominated soils of temperate and boreal forest ecoystems often leads to losses of oxidative enzyme activity, while activities in grassland soils dominated by glomeromycota and ascomycetes show little net response. Land use that leads to loss of soil organic matter tends to increase oxidative activities. Across ecosystems, soil organic matter content is not correlated with mean potential phenol oxidase and peroxidase activities. A multiple regression model that includes soil pH, mean annual temperature, mean annual precipitation and potential phenol oxidase activity accounts for 37% of the variation in soil organic matter (SOM) content across ecosystems (n = 63); a similar model for peroxidase activity describes 32% of SOM variance (n = 43). Analysis of residual variation suggest that suites of interacting factors create both positive and negative feedbacks on soil organic matter storage. Soils with high oxygen availability, pH and mineral activity tend to be substrate limited: high in situ oxidative activities limit soil organic matter accumulation. Soils with opposing characteristics are activity limited: low in situ oxidative activities promote soil organic matter storage.

Phenol oxidase, peroxidase and organic matter dynamics of soil

Enzyme stability and stabilization—Aqueous and non-aqueous environment

This paper reviews the best known techniques using circular dichroism spectroscopy such as conventional circular dichroism (i.e. electronic circular dichroism), magnetic circular dichroisms (magnetic vibrational circular dichroism, x-ray magnetic circular dichroism), fluorescence detected circular dichroism, near-infrared circular dichroism, vibrational circular dichroism, Fourier transform infrared circular dichroism, high pressure liquid chromatography circular dichroism, stopped-flow circular dichroism, and synchrotron radiation circular dichroism. Also, we have described here the most important applications of circular dichroism spectroscopy in structural biochemistry and nanoscience.

/pdf/circular-dichroism-techniques-biomolecular-and-50alihc3rh.pdf

Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses- A Review

This paper reviews the best-known differential scanning calorimetries (DSCs), such as conventional DSC, microelectromechanical systems-DSC, infrared-heated DSC, modulated-temperature DSC, gas flow-modulated DSC, parallel-nano DSC, pressure perturbation calorimetry, self-reference DSC, and high-performance DSC. Also, we describe here the most extensive applications of DSC in biology and nanoscience.

/pdf/differential-scanning-calorimetry-techniques-applications-in-7ozkshrju8.pdf

Differential Scanning Calorimetry Techniques: Applications in Biology and Nanoscience

Effective factors in thermostability of thermophilic proteins.

A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104

Binding of water-soluble N,N′,N″,N‴-tetramethyltetra-3,4-pyridinoporphyrazinatozinc(II)
				{[Zn(3,4-tmtppa)]4+} and N,N′,N″,N‴-tetramethyltetra-3,4-pyridinoporphyrazinatocobalt(II)
				{[Co(3,4-tmtppa)]4+} with calf thymus DNA has been investigated in 1 mM phosphate buffer and 5 mM NaCl at low ionic strength by UV-vis, fluorescence, and circular dichroism (CD) spectroscopic techniques, and also by the viscometric method. The appearance of a dramatic hypochromicity without any shift in the Q-band maximum of Zn(tmtppa) in the presence of DNA and a positive ellipticity in the visible CD of this porphyrazine complexed with DNA are definitive evidence of outside binding of this complex. It can be assumed that [Zn(3,4-tmtppa)]4+ in water is axially ligated by one H2O molecule. Therefore, this complex is inhibited from intercalation and binds externally. The interaction of [Co(3,4-tmppa)]4+ with DNA causes a decrease of the absorbance in the Q-band region of porphyrazine and a large red-shift. The visible CD of Co(tmtppa) complexed with DNA manifests a pattern of bisignate CD spectra, which possibly lead us to the coexistence of intercalation and outside binding modes. The binding constants were determined from the changes in the Q-band maximum of the porphyrazine spectra using SQUAD software. The values of K were (8.9 ± 0.3) × 104 and (2.3 ± 0.0) × 105 M−1 for [Co(3,4-tmtppa)]4+ and [Zn(3,4-tmtppa)]4+, respectively, at 27 °C. The higher affinity of the zinc complex towards DNA with respect to the cobalt complex was attributed to the coordination interaction as the major contributing factor, which enables superior interaction of the zinc complex with the DNA duplex. The thermodynamic parameters (ΔG°, ΔH°, ΔS°) were calculated from the van't Hoff equation at various temperatures. The enthalpy and entropy changes were determined to be: +39.6 ± 3.0 kJ mol−1 and +226.7 ± 10.5 J mol−1 K−1 for [Co(3,4-tmtppa)]4+ and +44.0 ± 3.3 kJ mol−1 and +249.6 ± 11.3 J mol−1 K−1 for [Zn(3,4-tmtppa)]4+. The positive and large values of the entropy and enthalpy suggest that both hydrophobic and electrostatic interactions may play an important role in the stabilization of the complex. The influence of the ionic strength was investigated. It was concluded that the apparent binding constants decrease with increasing [Na+] as predicted. Titration of DNA with Zn(tmtppa) produces moderate decreases in the solution-reduced viscosity (SRV), indicative of outside binding. The increase in the viscosity of DNA in the presence of the cobalt complex is related to the lengthening of the DNA helix due to the intercalation. The quenching of the DNA–ethidium bromide complex by the above-mentioned porphyrazines was investigated. The values of the quenching constants (KSV) and the rate constants of the quenching (kq) were determined by the Stern–Volmer equation.

Thermodynamic and spectroscopic study on the binding of cationic Zn(II) and Co(II) tetrapyridinoporphyrazines to calf thymus DNA: the role of the central metal in binding parameters

Bijan Ranjbar

Papers

Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses- A Review

Differential Scanning Calorimetry Techniques: Applications in Biology and Nanoscience

Effective factors in thermostability of thermophilic proteins.

A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104

Thermodynamic and spectroscopic study on the binding of cationic Zn(II) and Co(II) tetrapyridinoporphyrazines to calf thymus DNA: the role of the central metal in binding parameters