Purification and properties of a 35 kDa glycoprotein from spermathecal extract of Eyprepocnemis plorans (insecta, Orthoptera) with axonemal cytoskeleton disassembly activity

Andrea Giuffrida; Riccardo Focarelli; Raffaella Lampariello; Hubert Thole; Floriana Rosati

doi:10.1016/0965-1748(95)00095-X

Purification and properties of a 35 kDa glycoprotein from spermathecal extract of Eyprepocnemis plorans (insecta, Orthoptera) with axonemal cytoskeleton disassembly activity

Andrea Giuffrida, Riccardo Focarelli, Raffaella Lampariello, Hubert Thole, Floriana Rosati

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

9 Scopus citations

Abstract

A glycoprotein (gp35) was purified from spermathecal extract of the orthopteran Eyprepocnemis plorans by FPLC gel filtration. Using an in vitro assay, this protein was found to be the only spermathecal extract component capable of inducing modifications of the sperm flagellum similar to those observed in vivo. This biological activity is achieved during the course of sexual maturation. Intact gp35 migrated in SDS-PAGE as a doublet with 34 and 36 kDa components, becoming a single band after complete deglycosylation. The protein also has a unique N-terminus. Chemical deglycosylation revealed that the carbohydrate component accounts for about 10% of the total protein mass. Its pI was found to be slightly acidic. Radiolabeled gp35 bound the sperm surface with typical receptor-ligand kinetics.

Original language	English (US)
Pages (from-to)	347-354
Number of pages	8
Journal	Insect Biochemistry and Molecular Biology
Volume	26
Issue number	4
DOIs	https://doi.org/10.1016/0965-1748(95)00095-X
State	Published - Apr 1996
Externally published	Yes

Keywords

Cytoskeleton
Glycoprotein
Insects
Sperm
Spermatheca

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Insect Science

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10.1016/0965-1748(95)00095-X

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Purification and properties of a 35 kDa glycoprotein from spermathecal extract of Eyprepocnemis plorans (insecta, Orthoptera) with axonemal cytoskeleton disassembly activity. / Giuffrida, Andrea; Focarelli, Riccardo; Lampariello, Raffaella et al.

In: Insect Biochemistry and Molecular Biology, Vol. 26, No. 4, 04.1996, p. 347-354.

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

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title = "Purification and properties of a 35 kDa glycoprotein from spermathecal extract of Eyprepocnemis plorans (insecta, Orthoptera) with axonemal cytoskeleton disassembly activity",

abstract = "A glycoprotein (gp35) was purified from spermathecal extract of the orthopteran Eyprepocnemis plorans by FPLC gel filtration. Using an in vitro assay, this protein was found to be the only spermathecal extract component capable of inducing modifications of the sperm flagellum similar to those observed in vivo. This biological activity is achieved during the course of sexual maturation. Intact gp35 migrated in SDS-PAGE as a doublet with 34 and 36 kDa components, becoming a single band after complete deglycosylation. The protein also has a unique N-terminus. Chemical deglycosylation revealed that the carbohydrate component accounts for about 10% of the total protein mass. Its pI was found to be slightly acidic. Radiolabeled gp35 bound the sperm surface with typical receptor-ligand kinetics.",

keywords = "Cytoskeleton, Glycoprotein, Insects, Sperm, Spermatheca",

author = "Andrea Giuffrida and Riccardo Focarelli and Raffaella Lampariello and Hubert Thole and Floriana Rosati",

note = "Funding Information: Acknowledgements--This work was supported by a 60% grant from Ministero Universita' e Ricerca Scientifica e Tecnologica (M.U.R.S.T.)",

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doi = "10.1016/0965-1748(95)00095-X",

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AU - Giuffrida, Andrea

AU - Focarelli, Riccardo

AU - Lampariello, Raffaella

AU - Thole, Hubert

AU - Rosati, Floriana

N1 - Funding Information: Acknowledgements--This work was supported by a 60% grant from Ministero Universita' e Ricerca Scientifica e Tecnologica (M.U.R.S.T.)

PY - 1996/4

Y1 - 1996/4

N2 - A glycoprotein (gp35) was purified from spermathecal extract of the orthopteran Eyprepocnemis plorans by FPLC gel filtration. Using an in vitro assay, this protein was found to be the only spermathecal extract component capable of inducing modifications of the sperm flagellum similar to those observed in vivo. This biological activity is achieved during the course of sexual maturation. Intact gp35 migrated in SDS-PAGE as a doublet with 34 and 36 kDa components, becoming a single band after complete deglycosylation. The protein also has a unique N-terminus. Chemical deglycosylation revealed that the carbohydrate component accounts for about 10% of the total protein mass. Its pI was found to be slightly acidic. Radiolabeled gp35 bound the sperm surface with typical receptor-ligand kinetics.

AB - A glycoprotein (gp35) was purified from spermathecal extract of the orthopteran Eyprepocnemis plorans by FPLC gel filtration. Using an in vitro assay, this protein was found to be the only spermathecal extract component capable of inducing modifications of the sperm flagellum similar to those observed in vivo. This biological activity is achieved during the course of sexual maturation. Intact gp35 migrated in SDS-PAGE as a doublet with 34 and 36 kDa components, becoming a single band after complete deglycosylation. The protein also has a unique N-terminus. Chemical deglycosylation revealed that the carbohydrate component accounts for about 10% of the total protein mass. Its pI was found to be slightly acidic. Radiolabeled gp35 bound the sperm surface with typical receptor-ligand kinetics.

KW - Cytoskeleton

KW - Glycoprotein

KW - Insects

KW - Sperm

KW - Spermatheca

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JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

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ER -

Purification and properties of a 35 kDa glycoprotein from spermathecal extract of Eyprepocnemis plorans (insecta, Orthoptera) with axonemal cytoskeleton disassembly activity

Abstract

Keywords

ASJC Scopus subject areas

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