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  • The glycation of albumins (HSA and BSA) was studied by nano-LC coupled to a QTOF mass spectrometer. Non-enzymatic in vitro reaction products between albumin and ribose were identified. Besides well-known carboxymethyl lysine, new modifications were determined –creating mass shifts of 78 and 218. The origin of the first modification is discussed and its possible structure is presented. Another mass shift of 132 belonged to a Schiff base
  • The glycation of albumins (HSA and BSA) was studied by nano-LC coupled to a QTOF mass spectrometer. Non-enzymatic in vitro reaction products between albumin and ribose were identified. Besides well-known carboxymethyl lysine, new modifications were determined –creating mass shifts of 78 and 218. The origin of the first modification is discussed and its possible structure is presented. Another mass shift of 132 belonged to a Schiff base (en)
Title
  • Monotopic modifications derived from in vitro glycation of albumin with ribose
  • Monotopic modifications derived from in vitro glycation of albumin with ribose (en)
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  • Monotopic modifications derived from in vitro glycation of albumin with ribose
  • Monotopic modifications derived from in vitro glycation of albumin with ribose (en)
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  • RIV/67985823:_____/13:00394058!RIV14-GA0-67985823
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  • I, P(GA203/08/1428), P(GAP206/12/0453)
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  • 12
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  • 89501
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  • RIV/67985823:_____/13:00394058
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  • advanced glycation end product (AGE); albumin; CE-MS; glycation; LC-MS/MS (en)
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  • DE - Spolková republika Německo
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  • [4AACF1FCEEC0]
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  • Electrophoresis
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  • 34
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  • Mikšík, Ivan
  • Pataridis, Statis
  • Sedláková, Pavla
  • Šťastná, Zdeňka
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  • 000320385400007
issn
  • 0173-0835
number of pages
http://bibframe.org/vocab/doi
  • 10.1002/elps.201300014
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