کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1930876 1050532 2011 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Ribose sugars generate internal glycation cross-links in horse heart myoglobin
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Ribose sugars generate internal glycation cross-links in horse heart myoglobin
چکیده انگلیسی

Glycation of horse heart metmyoglobin with d-ribose 5-phosphate (R5P), d-2-deoxyribose 5-phosphate (dR5P), and d-ribose with inorganic phosphate at 37 °C generates an altered protein (Myo-X) with increased SDS–PAGE mobility. The novel protein product has been observed only for reactions with the protein myoglobin and it is not evident with other common sugars reacted over a 1 week period. Myo-X is first observed at 1–2 days at 37 °C along with a second form that is consistent in mass with that of myoglobin attached to several sugars. MALDI mass spectrometry and other techniques show no evidence of the cleavage of a peptide from the myoglobin chain. Apomyoglobin in reaction with R5P also exhibited this protein form suggesting its occurrence was not heme-related. While significant amounts of O2− and H2O2 are generated during the R5P glycation reaction, they do not appear to play roles in the formation of the new form. The modification is likely due to an internal cross-link formed during a glycation reaction involving the N-terminus and an internal amine group; most likely the neighboring Lys133. The study shows the unique nature of these common pentose sugars in spontaneous glycation reactions with proteins.


► Myoglobin is glycated by ribose and deoxyribose sugars.
► Heme reduction and heme loss due to glycation-generated H2O2.
► Internal cross-linking between N-terminus and Lys.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 407, Issue 1, 1 April 2011, Pages 191–196
نویسندگان
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