Le paysage, nouvel acteur du développement territorial

info:eu-repo/semantics/nonPublishe

Comparative study of the binding to human serum albumin of biliscopine (a new cholangiographic contrast medium) and five other contrast media

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Purification and preliminary characterization of protease B from Saccharomyces cerevisiae

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Protease B from Saccharomyces cerevisiae. Purification and characterization

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Traditionnal management of the rural areas in Wallonia (Belgium)' in Nature Conservation: Concepts and practice

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Binding capacities of various analogues of S-adenosyl-L-homocysteine to protein methyltransferase II from human erythrocytes

A series of analogues of S-adenosyl-L-homocysteine, modified mainly in the amino acid portion of the molecule, have been synthesized. All were found to be competitive inhibitors of protein methyltransferase II from human erythrocytes. S-adenosyl-L-homocysteine remains however by far the most effective inhibitor of the methylase. © 1979 Birkhäuser Verlag.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Alkaline isomerization of horse and yeast cytochromes C

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Inhibition of protein methyltransferases II from human erythrocytes by S-adenosyl-L-homocysteine and structurally related molecules

Protein methyltransferase II catalyses the transformation of carboxyl functions of proteins in their methyl-esters. The responsible enzyme was recently obtained from horse erythrocytes and structurally analysed. To characterise the active side of protein methyltransferase II, different analogues of S-adenosyl-L-homocystein (the natural inhibitor of methylases) were synthesized and their binding to the enzyme was measured. S-adenosyl-L-homocystein was found to be the most active inhibitor (Ki - 0.1 M). Modifications of the sulphur atom reduced the Ki value. More essential losses in inhibition were found after the use of amino acid substitutes in the natural inhibitors. Most (probably all) of the examined compounds were inhibitors. It was therefore concluded that the amino acid part of S-adenosyl-L-homocystein contributes to the enzyme binding, though a contribution can be expected from the base and ribose units.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Isolation and characterization of chicken (Gallus gallus) and penguin (Aptenodytes forsteri) myoglobins

Methods describing isolation, purification and characterization of two avian myoglobins are reported. Chicken myoglobin was extracted at 55 to 90 p. cent ammonium sulfate saturation, while penguin myoglobin was isolated by low temperature fractionation using ethanol in the presence of metallic ions. Both were purified by gel filtration and chromatography on CM Sephadex and their homogeneity was tested by zone electrophoresis with different gels. The amino acid compositions have been determined. Chicken hemoprotein appears very similar to previously studied myoglobin, but penguin hemoprotein differs significantly, essentially by a higher amount of methionine. Both proteins have glycine as the aminoterminal residue. The molar extinction coefficients and the reduced mean residue optical rotation were found to be identical. © 1972.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Penguin (Aptenodytes forsteri) myoglobin. A 70 residue N-terminal sequence

SCOPUS: ar.jinfo:eu-repo/semantics/publishe