Hydrophobic interaction chromatography of autoproteolysis products of human seminal plasma

Mazzini, María N.; Giacomo, María Angélica Di; Cerezo, Alberto S.

doi:10.1002/bmc.1130020405

Cited by 2 publications

(1 citation statement)

References 12 publications

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“…Amino acid analysis was performed as described elsewhere (17), using a Technicon Sequential Multi-Sample Amino Acids Analyzer TM S2 and the amino acids obtained by peptide hydrolysis with 6 M HCl at 105 o C for 24 h. Amino acids were purified with Amberlite IR-120 before analysis.…”

Section: Amino Acid Analysismentioning

confidence: 99%

Proteolytic release and partial characterization of human sperm-surface glycopeptides

Tortorella¹,

Konrath²,

Mazzini³

et al. 1997

Braz J Med Biol Res

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Sperm-surface glycopeptides were obtained from intact sperm membranes after proteolytic release by different enzymatic treatments such as autoproteolysis, trypsin, papain and pronase. Glycopeptides were isolated, their properties and composition were examined, and their monosaccharide and amino acid constituents were characterized. The monosaccharides identified were fucose, mannose, galactose, N-acetylglucosamine, and N-acetylgalactosamine, which form part of more than one type of oligosaccharide units. Autoproteolytic treatment mainly provided O-glycosidic type oligosaccharides, while a mixture of O-and N-glycosidic oligosaccharides was obtained in variable proportions when treated with trypsin, papain or pronase. The highest degree of peptide cleavage was obtained with pronase. Despite the higher yields reached with trypsin, these glycopeptides contain the lowest percentage of oligosaccharide chains. Proteolytic treatment provides a simple, rapid procedure for the isolation of glycopeptides from the sperm surface.

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Section: Amino Acid Analysismentioning

confidence: 99%

Proteolytic release and partial characterization of human sperm-surface glycopeptides

Tortorella¹,

Konrath²,

Mazzini³

et al. 1997

Braz J Med Biol Res

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Lopes

Mazzini

Tortorella

et al. 1998

Glycoconjugate Journal

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Affinity chromatography on Concanavalin-A Sepharose, followed by gel filtration and hydrophobic interaction chromatography, permits the isolation of low molecular weight N-glycosidically linked oligomannosidic glycopeptides (MGp) from the autoproteolysis products of human seminal plasma. The monosaccharide composition of MGp showed only mannose, N-acetylglucosamine and a small amount of galactose. Structural studies were carried out by methylation analysis and chromium trioxide oxidation, and results were consistent with the structures accepted for high-mannose N-glycans. MGp was capable of inhibiting the sperm acrosomal exocytosis mediated by sperm-surface receptors. These data suggest that MGp act as a "decapacitation" factor preventing premature sperm exocytosis.

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Hydrophobic interaction chromatography of autoproteolysis products of human seminal plasma

Cited by 2 publications

References 12 publications

Proteolytic release and partial characterization of human sperm-surface glycopeptides

Proteolytic release and partial characterization of human sperm-surface glycopeptides

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