[Complete structure of three galactoxyloglucans (amyloids) from seeds]. / Etude complémentaire de la structure de trois galactoxyloglucanes (amyloïdes) de graines

D-Galacto-D-xylo-D-glucans (amyloids) from Balsamina, Tropaeolum, and Tamarindus seeds behave in a similar manner in the presence of various glycosidase preparations: slow depolymerization by enzymes from several germinated or non-germinated seeds, and hydrolysis into monosaccharides and oligosaccharides by commercial cellulase and hemicellulase preparations from fungi. A purified cellulase from Penicillium notatum gave a dialyzable fraction almost exclusively composed of alpha-D-xylopyranosyl-(1 leads to 6)-D-glucose residues and a nondialyzable fraction composed of chains of beta-D-(1 leads to 4) [With some (1 leads to 3)]-glucopyranosyl residues; beta-D-galactopyranosyl-(1 leads to 2)-alpha-D-xylosyl groups are linked to some of the beta-D-glucosyl residues at O-6. The presence of (1 leads to 3)-linkages in the D-glucan chain of the Balsamina was verified by methylation and sequential periodate oxidation-borohydride reduction; the distribution of the substituents on the D-glucan chain is not regular. The main D-glucan backbone, where the beta-D-glucosyl residues are partly linked at O-6 to beta-D-galactosyl-(1 leads to 2)-D-xylosyl groups, is linked to D-glucan chains where almost all the D-glucose units are linked at O-6 by one alpha-D-xylosyl group. The presence of 3,6-di-O-methyl-D-glucose after permethylation and hydrolysis suggests that the xyloglucan chains are linked to O-2 of the D-glucosyl units of the galactoxyloglucan backbone.

[alpha-L-Rhamnosidase from Fagopyrum esculentum: purification and some properties (author's transl)]. / alpha-L-Rhamnosidase de Fagopyrum esculentum. Purification et quelques propriétés

An alpha-L-rhamnosidase from the seeds of Fagopyrum esculentum (saracen corn) has previously been identified, and the effect of the enzyme on rhamnoisic bonds has been studied with various flavonoid glycosides. This alpha-L-rhamnosidase can be useful in structural studies, and a preliminary report of this study has appeared. The present paper describes the extensive purification of the enzyme and the determination of its properties. The purification involved extraction, ammonium sulfate fractionation and chromatography on Sephadex G 75, DEAE-Sephadex and Ultrogel AcA-44. The alpha-L-rhamnosidase was purified about 9600 fold and the final enzyme preparation was practically pure according to the criteria of disc electrophoresis. The molecular weight of this alpha-L-rhamnosidase, calculated from data obtained by disc gel electrophoresis and gel filtration, was about 70 000. Isoelectric focusing established the isoelectric point to be 3.7. The behaviour of the enzyme on a concanavalin-A-Sepharose column suggests the presence of residues resembling alpha-D-mannose or alpha-D-glucose in the protein. The various kinetic parameters, Kcat, Km and the Kcat/Km ratio have been determined at pH 5 on the following substrates: p-nitrophenyl-alpha-L-rhamnoside and rutinose (6-O-alpha-L-rhamnosyl-D-glucopyranose). All kinetics exhibit a Michaelian behaviour and the Km for the former substrate was 0.33 mM and for the latter, 2.2 mM. The Kcat/Km ratio corroborates the greater specificity of the enzyme for p-nitrophenyl-alpha-L-rhamnoside. L-Rhamnose, L-lyxose, 6-deoxy-D-glucose and methyl-alpha-D-mannoside were shown to behave strictly as competitive inhibitors of alpha-L-rhamnosidase activity; it seems that the methyl group of L-rhamnose is important for substrate binding to the enzyme.

[Metabolism of Helix pomatia polygalacturonase]. / Mode d'action de la polygalacturonase du suc d'Helix pomatia

The reaction pattern of the polygalacturonase from Helix pomatia juice has been studied. Hydrolysis of pectic acid occurs in a random manner. Oligogalacturonic acids are hydrolyzed in a sequential process, starting from the non-reducing end. This behavior is different from that of other endopolygalacturonases, which split these latter substrates both randomly and in a stepwise way from the reducing end.

[Alpha-mannosidase activity of different human biological fluids]. / Activité alpha-mannosidasique de quelques liquides biologiques chez l'Hommone

Two distinct alpha-mannosidases have been found in biological fluids by investigating the effect of pH on activity, the effect of Co2+ and Zn2+ and by determining the Michaelis constant. The two enzymes are designated as S, predominating in serum (optimum pH about 5.6) and U, predominating in urine (optimum pH about 4.2). In cerebro-spinal fluid, the amount of alpha-mannosidase S is almost the same as that of alpha-mannosidase U. Alpha-mannosidase S activity in sera is significantly higher in children than in adults.

[Influence of parenteral injection of trehalose on mammals with different trehalase levels]. / Influence de l'injection parentérale de tréhalose sur des mammifères à équipements tréhalasiques distincts

Administration of trehalose by parenteral route to mammals (Guinea-pig and rabbit) equipped with Kidney trehalase is followed by rapid hydrolysis of the disaccharide which is excreted in urine only in very low amounts. When the animal under investigation has not trehalase in the kidney (rat), practically the total amount of trehalase is excreted in urine. Perfusion of kidney in rabbit confirms the very rapid hydrolysis of trehalose by this organ.

[Influence of parenterally injected trehalose in mammals having trehalase activity at different sites]. / Influence de l'injection parentérale de tréhalose chez des mammifères possédant une activité tréhalasique diversement localisée

When trehalose is injected via parenteral pathway into animals lacking kidney trehalase (rat), more than 75 per cent of this disaccharide is eliminated in urine. When the injected animals possess an active kidney trehalase (guinea-pig, rabbit), there is only a low urinary trehalose excretion. Moreover, in rabbit, a marked hyperglycaemia is observed which is due to the rapid hydrolysis of trehalose by kidney trehalase.