Loi (italienne) du 12 juin 1902 (n° 185), édictant des dispositions sur la protection et la conservation des monuments et objets ayant une valeur d'art et d'antiquité, notice et traduction par M. Paul Carpentier,...

[Loi. 1902-06-12]

Openness and privacy in Ontario: an evaluation of the implementation of FIPPA : (The Freedom of Information and Protection of Privacy Act, 1987, Chapter 25 and Ontario Regulation 532/87) /

Since the early 1970's, Canadians have expressed many concerns about the growth of government and its impact on their daily lives. The public has requested increased access to government documents and improved protection of the personal information which is held in government files and data banks. At the same time, both academics and practitioners in the field of public administration have become more interested in the values that public servants bring to their decisions and recommendations. Certain administrative values, such as accountability and integrity, have taken on greater relative importance. The purpose of this thesis is to examine the implementation of Ontario's access and privacy law. It centres on the question of whether or not the Freedom of Information and Protection of Privacy Act, 1987, (FIPPA) has answered the demand for open access to government while at the same time protecting the personal privacy of individual citizens. It also assesses the extent to which this relatively new piece of legislation has made a difference to the people of Ontario. The thesis presents an overview of the issues of freedom of information and protection of privacy in Ontario. It begins with the evolution of the legislation and a description of the law itself. It focuses on the structures and processes which have been established to meet the procedural and administrative demands of the Act. These structures and processes are evaluated in two ways. First, the thesis evaluates how open the Ontario government has become and, second, it determines how Ill carefully the privacy rights of individuals are safeguarded. An analytical framework of administrative values is used to evaluate the overall performance of the government in these two areas. The conclusion is drawn that, overall, the Ontario government has effectively implemented the Freedom of Information and Protection of Privacy Act, particularly by providing access to most government-held documents. The protection of individual privacy has proved to be not only more difficult to achieve, but more difficult to evaluate. However, the administrative culture of the Ontario bureaucracy is shown to be committed to ensuring that the access and privacy rights of citizens are respected.

Aspects of the hemes and modulation of hydrogen donors in catalases from bovine liver, yeast, and escherichia coli

Catalase is the enzyme which decomposes hydrogen peroxide to water and oxygen. Escherichia coli contains two catalases. Hydroperoxidase I (HPI) is a bifunctional catalase-peroxidase. Hydroperoxidase II (HPII) is only catalytically active toward H202. Expression of the genes encoding these proteins is controlled by different regimes. HPJI is thought to be a hexamer, having one heme d cis group per enzymatic subunit. HPII wild type protein and heme containing mutant proteins were obtained from the laboratory of P. Loewen (Univ. of Manitoba). Mutants constructed by oligonucleotidedirected mutagenesis were targeted for replacement of either the His128 residue or the Asn201 residue in the vicinity of the HPII heme crevice. His128 is the residue thought to be analogous to the His74 distal axial ligand of the heme in the bovine liver enzyme, and Asn201 is believed to be a residue critical to the function of the enzyme because of its role in orienting and interacting with the substrate molecule. Investigation of the nature of the hemes via absorption spectroscopy of the unmodified catalase proteins and their derived pyridine hemochromes showed that while the bovine and Saccharomyces cerevisiae catalase enzymes are protoheme-containing, the HPII wild type protein contains heme d, and the mutant proteins contain either solely protoheme, or heme d-protoheme mixtures. Cyanide binding studies supported this, as ligand binding was monophasic for the bovine, Saccharomyces cerevisiae, and wild type HPII enzymes, but biphasic for several of the HPII mutant proteins. Several mammalian catalases, and at least two prokaryotic catalases, are known to be NADPH binding. The function of this cofactor appears to be the prevention of inactivation of the enzyme, which occurs via formation of the inactive secondary catalase peroxide compound (compound II). No physiologically plausible scheme has yet been proposed for the NADPH mediation of catalase activity. This study has shown, via fluorescence and affinity chromatography techniques, that NADPH binds to the T (Typical) and A (Atypical) catalases of Saccharomyces cerevisiae, and that wild type HPII apparently does not bind NADPH. This study has also shown that NADPH is unlike any other hydrogen donor to catalase, and addresses its features as a unique donor by proposing a mechanism whereby NADPH is oxidized and catalase is protected from inactivation via the formation of protein radical species. Migration of this radical to a position close to the NADPH is also proposed as an adjunct hypothesis, based on similar electron migrations that are known to occur within metmyoglobin and cytochrome c peroxidase when reacted with H202. Validation of these hypotheses may be obtained in appropriate future experiments.