High impact information on L-Threose

• Assays were linear over 1 h, and most activity was seen after a 2 d incubation of 5 mM L-threose and 10 mM alpha-N-acetyl-lysine (N-Ac-Lys) or 10 mg/mL RNase A [1].
• This was confirmed by incubating a preparation of [1-14C]L-tetrose (a mixture of 40% L-threose and 45% L-erythrose) with both the pure aldose reductase and crude lens extracts followed by the subsequent identification of the [1-14C]L-threitol formed by thin layer chromatography [2].
• Assays with human recombinant aldose reductase and with human lens cortical and nuclear extracts all exhibited sorbinil-inhibitable aldose reductase activity with L-threose as substrate [2].
• In the present study, the degradation of L-threose at pH 7.0 alone, in the presence of N-alpha-acetyl-L-lysine, and at pH 2.0 alone at 37 degrees C was investigated by identification of some of the products produced in the reactions by means of GLC and GLC-MS [3].
• Protein modification by the degradation products of ascorbate: formation of a novel pyrrole from the Maillard reaction of L-threose with proteins [4].

Gene context of L-Threose

• These data confirm a rapid reactivity of L-threose with lens protein and argue that glycation would occur in vivo in spite of the presence of aldose reductase [2].

Analytical, diagnostic and therapeutic context of L-Threose

• To determine whether L-threose was formed in the lens, the sugars in a TCA-soluble extract from human lenses were reduced to polyols with NaBH4, acetylated and analysed by gas-liquid chromatography [2].
• 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 [5].

References