Deglycosylation of glycoproteins by trifluoromethanesulfonic acid

Edge, Albert S.B.; Faltynek, Connie R.; Hof, Liselotte; Reichert, Leo E.; Weber, Peter

doi:10.1016/0003-2697(81)90168-8

Cited by 714 publications

(341 citation statements)

References 27 publications

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“…Pronase and trypsin digestion, heat treatment and treatment with 8-mercaptoethanol and periodate of the purified antigen were done as described by Vennegoor et al (1985). Treatment with trifluoromethanesulphonic acid was done according to Edge et al (1981). The binding of MAb F47-9 to the treated antigen preparations was then tested in a dot-blot assay, in which the preparations (1.3 pg ml-l) were coated in serial dilutions onto nitrocellulose filters (0.45 ~L M pore size, Schleicher and Schull).…”

Section: Methodsmentioning

confidence: 99%

Purification and Characterization of a 36 kDa Antigen of Mycobacterium leprae

Wit

Klatser

1988

Microbiology

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A 36 kDa antigen of Mycobacterium leprae was purified by phenol biphasic partition followed by preparative SDS-PAGE. The purified antigen appeared as a single band in SDS-PAGE and eluted as a single peak in ion-exchange chromatography. The antigen comprised epitopes which were cross-reactive with M . tuberculosis, as well as a species-specific epitope (recognized by MAb F47-9). Different treatments of the 36 kDa antigen suggested it to be largely protein in nature; the amino acid composition of 81 % of the antigen was determined. A majority of sera from leprosy patients contained antibodies recognizing the 36 kDa antigen.

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Section: Methodsmentioning

confidence: 99%

Purification and Characterization of a 36 kDa Antigen of Mycobacterium leprae

Wit

Klatser

1988

Microbiology

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“…They were then subjected to solvolysis [28] by dissolving 5 mg of lyophilized proteins in 1n2 ml of a TFMSA\anisole (2 : 1, v\v) mixture (ICN, St. Laurent, Que! bec, Canada) and incubating on ice for 2 h with gentle mixing.…”

Section: Reduction and Carboxymethylationmentioning

confidence: 99%

Biochemical analysis of a bladder-cancer-associated mucin: structural features and epitope characterization

Bergeron

LaRue

Fradet

1997

Biochemical Journal

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Three monoclonal antibodies (mAbs), M344, M300 and M75, were shown to define a unique tumour-associated antigen (TAA) of superficial bladder tumours. The antigenic determinants are expressed on a very-high-molecular-mass component and, in about 50 % of the positive samples, one determinant is also detected on a 62 kDa molecular species, observed only under reducing conditions. The objectives of the present study were to characterize further this TAA by analysing (1) the biochemical nature of the epitopes recognized by the three mAbs, and (2) the biochemical and structural features of the molecule bearing them. The antigenicity was resistant to heat denaturation, trypsin and α-chymotrypsin treatments but highly sensitive to papain and Pronase digestion. NaIO % oxidation decreased reactivity to mAbs M344 and M300 but enhanced reactivity to mAb M75. The three determinants were insensitive to β-galactosidase and α--fucosidase but were sensitive to Vibrio cholerae neuraminidase.

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“…PRG was deglycosylated by a modification of the method described by Edge et al (1981). A 1 ml portion of anisole (Aldrich Chemical Co.) and 2ml of trifluoromethanesulphonic acid (Aldrich) were cooled to 0°C, and then 1 ml of this solution was added to 7mg of PRG in a 2ml Reactivial (Pierce Chemical Co.).…”

Section: Experimental Procedures Preparation Of Prg and D-prgmentioning

confidence: 99%

Masticatory lubrication. The role of carbohydrate in the lubricating property of a salivary glycoprotein-albumin complex

Hatton¹,

Loomis²,

Levine³

et al. 1985

Biochemical Journal

131

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We report for the first time a masticatory-lubrication assay system to assess the lubricating properties of salivary constituents. The lubricating ability of the prolinerich glycoprotein (PRG) of parotid saliva was enhanced by human serum albumin. The interactive effect of albumin was abolished by chemically deglycosylating the glycoprotein. Fluorescence spectroscopy with a hydrophobic probe verified the existence of a PRG-albumin complex and demonstrated that deglycosylation of the PRG altered the nature of its interaction with albumin.

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Deglycosylation of glycoproteins by trifluoromethanesulfonic acid

Cited by 714 publications

References 27 publications

Purification and Characterization of a 36 kDa Antigen of Mycobacterium leprae

Purification and Characterization of a 36 kDa Antigen of Mycobacterium leprae

Biochemical analysis of a bladder-cancer-associated mucin: structural features and epitope characterization

Masticatory lubrication. The role of carbohydrate in the lubricating property of a salivary glycoprotein-albumin complex

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