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The continuous accumulation of AGEs is associated with severe diabetes and its associated ailments. Saccharides with their reducing ends can glycate amino acid side chains of proteins, among them glucose is well\u2010known for its potent glycating capability. However, other reducing sugars can be more reactive glycating agents than glucose. The D\u2010ribose is a pentose sugar\u2010containing an active aldehyde group in its open form and is responsible for affecting the biological processes of the cellular system. D\u2010ribose, a key component of many biological molecules, is more reactive than most reducing sugars. Protein glycation by reducing monosaccharides such as D\u2010ribose promotes the accelerated formation of AGEs that could lead to cellular impairments and dysfunctions. Also, under a physiological cellular state, the bioavailability rate of D\u2010ribose is much higher than that of glucose in diabetes, which makes this species much more active in protein glycation as compared with D\u2010glucose. Due to the abnormal level of D\u2010ribose in the biological system, the glycation of proteins with D\u2010ribose needs to be analyzed and addressed carefully. In the present study, human immunoglobulin G (IgG) was isolated and purified via affinity column chromatography. D\u2010ribose at 10\u00a0and 100\u2009mM concentrations was used as glycating agent, for 1\u201312\u2009days of incubation at 37\u00b0C. The postglycation changes in IgG molecule were characterized by UV\u2010visible and fluorescence spectroscopy, nitroblue tetrazolium assay, and various other physicochemical analyses for the confirmation of D\u2010ribose mediated IgG glycation.<\/jats:p>","DOI":"10.1002\/cbf.3722","type":"journal-article","created":{"date-parts":[[2022,6,16]],"date-time":"2022-06-16T04:20:15Z","timestamp":1655353215000},"page":"526-534","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Nonenzymatic glycosylation of isolated human immunoglobulin\u2010G by D\u2010ribose"],"prefix":"10.1002","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1215-0279","authenticated-orcid":false,"given":"Saheem","family":"Ahmad","sequence":"first","affiliation":[{"name":"Department of Medical Laboratory Sciences, College of Applied Medical Sciences University of Hail Hail Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Khalid","family":"Al\u2010Shaghdali","sequence":"additional","affiliation":[{"name":"Department of Medical Laboratory Sciences, College of Applied Medical Sciences University of Hail Hail Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shahnawaz","family":"Rehman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, S.S. 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