A 34-kilodalton polypeptide is associated with 1,3-β-glucan synthase activity from the fungus Saprolegnia monoica

Vincent Bulone; Michel Fèvre

doi:10.1111/j.1574-6968.1996.tb08328.x

A 34-kilodalton polypeptide is associated with 1,3-β-glucan synthase activity from the fungus Saprolegnia monoica

Vincent Bulone, Michel Fèvre

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-β-glucan synthase activity were isolated by glycerol gradient centrifugation of Chaps-solubilized proteins from the fungus Saprolegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified with 1,3-β-glucan synthase during enzyme purification. This antiserum adsorbs the enzyme activity as well as the 48- and 50-kDa polypeptides. These results indicate that the 34-kDa peptide is a component of the multisubunit protein complex involved in 1,3-β-glucan synthase activity.

Original language	English
Pages (from-to)	145-150
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	140
Issue number	2-3
DOIs	https://doi.org/10.1111/j.1574-6968.1996.tb08328.x
Publication status	Published - Jul 1996
Externally published	Yes

Keywords

1,3-β-Glucan synthase
Antibody
Polypeptide
Saprolegnia

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10.1111/j.1574-6968.1996.tb08328.xLicence: In Copyright

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title = "A 34-kilodalton polypeptide is associated with 1,3-β-glucan synthase activity from the fungus Saprolegnia monoica",

abstract = "Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-β-glucan synthase activity were isolated by glycerol gradient centrifugation of Chaps-solubilized proteins from the fungus Saprolegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified with 1,3-β-glucan synthase during enzyme purification. This antiserum adsorbs the enzyme activity as well as the 48- and 50-kDa polypeptides. These results indicate that the 34-kDa peptide is a component of the multisubunit protein complex involved in 1,3-β-glucan synthase activity.",

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year = "1996",

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AU - Bulone, Vincent

AU - Fèvre, Michel

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AB - Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-β-glucan synthase activity were isolated by glycerol gradient centrifugation of Chaps-solubilized proteins from the fungus Saprolegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified with 1,3-β-glucan synthase during enzyme purification. This antiserum adsorbs the enzyme activity as well as the 48- and 50-kDa polypeptides. These results indicate that the 34-kDa peptide is a component of the multisubunit protein complex involved in 1,3-β-glucan synthase activity.

KW - 1,3-β-Glucan synthase

KW - Antibody

KW - Polypeptide

KW - Saprolegnia

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AN - SCOPUS:0030200477

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ER -

A 34-kilodalton polypeptide is associated with 1,3-β-glucan synthase activity from the fungus Saprolegnia monoica

Abstract

Keywords

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