Matrix-assisted laser desorption/ionization mass spectrometric studies on protein glycation. 2. The reaction of ribonuclease with hexoses

Lapolla, Annunziata; Baldo, L.; Aronica, Rosaria; Gerhardinger, Chiara; Fedele, Domenico; Elli, Giuseppe; Seraglia, Roberta; Catinella, Silvia; Traldi, Pietro

doi:10.1002/bms.1200230502

Cited by 32 publications

(25 citation statements)

References 20 publications

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“…In the Odetti et al case both the glycated protein and propagators were measured, whereas in our case only the protein was studied. We made some further studies devoted to the in vitro glycation of various proteins with several sugars (Lapolla et al, 1994(Lapolla et al, , 1996a. Since the results turned out to be similar to those mentioned above, we are confident about the validity of MALDI-MS for studying protein glycation.…”

Section: Maldi-ms In the Study Of In Vitro Glycated Proteinssupporting

confidence: 65%

Detection of Glycated and Glyco‐Oxidated Proteins

2006

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Section: Maldi-ms In the Study Of In Vitro Glycated Proteinssupporting

confidence: 65%

Detection of Glycated and Glyco‐Oxidated Proteins

2006

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“…In previous investigations on protein glycation, under both in vitro 11,12 and in vivo [13][14][15] conditions, the MALDI 16 technique has revealed itself to be a valuable tool. Its sensitivity, specificity and mass accuracy not only yield the number of glucose molecules condensing on a specific protein, but also supply information on the dehydration/ oxidation levels of the glycated products.…”

mentioning

confidence: 98%

Direct evaluation of glycated and glyco-oxidized globins by matrix-assisted laser desorption/ionization mass spectrometry

Lapolla¹,

Fedele²,

Plebani³

et al. 1999

Rapid Commun. Mass Spectrom.

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Matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) has been applied to achieve a qualitative and quantitative evaluation of glycated globins on a wide number of healthy and diabetic subjects. The method allowed us to establish that both alpha- and beta-globins are glycated and that, in addition to simply glycated products, other species are detected. Investigations by different sample treatments and by analysis of the glycated beta-globin fraction obtained by preparative chromatography indicated that these species correspond to glyco-oxidized globins. Consequently MALDI-MS can be validly employed to evaluate not only the glycation level, but also the degree of oxidative stress. The percentages of glycated and glycooxidized species were calculated from the related MALDI spectra by the measurement of the related peak areas, without any other treatment of data. A linear relationship between HbA1c values and the total percentage of glycated and glyco-oxidized globins has been found, and its slope (< 1) has been rationalized by the uncorrected evaluation of glycated globins content in the standard samples employed for HbA1c measurements.

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“…LapoUa et al (21) detected similar addition products with RNase and f~ctose using MALDI spectroscopy, with up to 5 fructose units added. While these adducts may represent additions to different lysine residues, our data suggest that only one or two sites could be sufficient for this number of fructose residues added.…”

Section: Vol 40 No 2 1996mentioning

confidence: 89%

“…Therefore, the main purposes of the present investigation were to detect the early glycation products and also to determine their relative molecular mass by non-invasive methods, such as mass spectrometry. By employing a combination of HPLC, FABMS and ESIMS, precise determination of the modified or glycated peptides or proteins has been achieved by other investigators (20,21).…”

Section: Vol 40 No 2 1996mentioning

confidence: 99%

Rapid assessment of early glycation products by mass spectrometry

1996

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Summary:In order to detect the early glycation products, we have reacted a model peptide (tboc-lys-ala-ala) with L-threose (a degradation product of ascorbic acid) and analyzed the reaction products by a combination of HPLC and mass spectrometry. Amino group modification, as observed by a fluorescamine assay, indicated complete modification after 3 days of incubation with a 10-fold excess of threose. As much as 60% of the adducts were acid labile and only 4% of the adducts could be observed by amino acid analysis. However, Fast atom bombardment mass spectrometry (FABMS) of the samples incubated for 6 hr showed relative molecular masses consistent with the formation of adducts corresponding to the addition of one and two molecules of L-threose to the peptide. Likewise, samples incubated for 12 hr showed peptide adducts with two and three L-threoses. The number of threose molecules added to the peptide was also confLrrned from the FABMS analysis by using [1-13C]-threose as the glycating agent.

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Matrix-assisted laser desorption/ionization mass spectrometric studies on protein glycation. 2. The reaction of ribonuclease with hexoses

Cited by 32 publications

References 20 publications

Detection of Glycated and Glyco‐Oxidated Proteins

Detection of Glycated and Glyco‐Oxidated Proteins

Direct evaluation of glycated and glyco-oxidized globins by matrix-assisted laser desorption/ionization mass spectrometry

Rapid assessment of early glycation products by mass spectrometry

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