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4 results on '"B, Mayet"'

1. Aspergillus niger van Tieghem mannosylation: polyprenylphosphate mannosyltransferase specificity

Author

R Létoublon, B Mayet, J Frot-Coutaz, and R Got

Subjects
Biochemistry, QD415-436
Abstract

Aspergillus niger van Tieghem microsomes contain an enzyme that catalyzes mannose transfer from GDP-mannose to polyprenylphosphate. The studies of the specificity of this enzyme for both the sugar donor (nucleoside diphosphate sugar) and the acceptor (polyprenylphosphates that were made available to the enzyme by means of the fusion of acceptor-loaded liposomes with the microsomal membranes) gave the following results. i) All the polyprenylphosphates from C15 to C120 were acceptors except retinylphosphate. ii) The specificity of the enzyme for both the sugar and the base is very strict.

Published
1982
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2. Subcellular distribution of phospholipids and of polyprenyl phosphate in Aspergillus niger van tieghem

Author

R. Letoublon, B. Mayet, R. Got, Claude Nicolau, and J. Frot-Coutaz

Subjects
chemistry.chemical_classification, Chromatography, biology, Aspergillus niger, Biophysics, Phospholipid, biology.organism_classification, Phosphate, Biochemistry, chemistry.chemical_compound, Endocrinology, Enzyme, chemistry, Mannosylation, Cardiolipin, Microsome, Cell fractionation
Abstract

Growth of Aspergillus niger Van Tieghem in presence of 32p1 was followed by cell fractionation; the subcellular fractions were identified using marker enzymes and their phospholipid content was analyzed. Microsomes are characterized by high PC and PS values, whereas the largest amount of cardiolipin is recovered in the mitochondria. Polyprenyl phosphate was found mainly in mitochondria (46%) (microsomal content: 38%) and, more precisely, the highest ratio was in the outer membrane. This situation raises the problem of polyprenyl phosphate transfer from mitochondria to microsomes where the enzyme responsible for polyprenyl phosphate mannosylation is located.

Published
1982
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3. [The specifics of home care].

Author

Milord C, Delage S, Dagort O, Fioramonti C, Hamet S, Mayet B, Vigier N, Herbinière L, and Michard E

Subjects
France, Health Services Needs and Demand, Humans, Organizational Objectives, Community Health Nursing organization & administration, Home Care Services organization & administration, Patient Care Team organization & administration
Published
2008

4. Aspergillus niger van Tieghem mannosylation: polyprenylphosphate mannosyltransferase specificity.

Author

Létoublon R, Mayet B, Frot-Coutaz J, and Got R

Subjects
Chromatography, Thin Layer, Kinetics, Liposomes, Phosphatidylcholines, Phosphatidylethanolamines, Substrate Specificity, Aspergillus niger enzymology, Hexosyltransferases metabolism, Mannosyltransferases metabolism, Microsomes enzymology
Abstract

Aspergillus niger van Tieghem microsomes contain an enzyme that catalyzes mannose transfer from GDP-mannose to polyprenylphosphate. The studies of the specificity of this enzyme for both the sugar donor (nucleoside diphosphate sugar) and the acceptor (polyprenylphosphates that were made available to the enzyme by means of the fusion of acceptor-loaded liposomes with the microsomal membranes) gave the following results. i) All the polyprenylphosphates from C15 to C120 were acceptors except retinylphosphate. ii) The specificity of the enzyme for both the sugar and the base is very strict.

Published
1982

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