In vitro synthesis of hemoglobin A<sub>Ic</sub>

Flückiger, Rudolf; Winterhalter, Kaspar H.

doi:10.1016/0014-5793(76)80969-6

Cited by 470 publications

(137 citation statements)

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“…Hydrolysation under weak acidic conditions caused 5-hydroxymethylfurfural (HMF) to be formed, which was estimated by the thiobarbituric acid method [9]. Hydrolysation in 6 N hydrochloric acid caused further destruction and various products including e-N-(-2-furoylmethyl)-L-lysine (furosine) were formed, which were estimated by high performance liquid chromatography according to the method of Schleicher and Wieland [10].…”

Section: Methodsmentioning

confidence: 99%

Glycosylation of human fibrinogen in vivo

et al. 1985

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Summary.Fibrinogen was purified from plasma from 22 nondiabetic and 26 poorly controlled Type I (insulin-dependent) diabetic subjects. In non-diabetic subjects, 0.95+0.17mol glucose was bound per mol fibrinogen, whereas in the diabetic subjects 1.33 + 0.21 mol glucose was bound per tool fibrinogen (mean + SD, p < 0.001). Comparison of the amount of bound glucose, when estimated by two different methods, suggested that lysine is the site of glycosylation. It is currently unknown whether this increased glycosylation of fibrinogen alters its function.Key words: Fibrinogen, glycosylation, Type I diabetes.Glucose has been shown to bind non-enzymatically and irreversibly to all types of protein through Schiff-base formation and Amadori re-arrangement to a ketoamine [1]. This glycosylation appears to be dependent on the duration of exposure and glucose concentration in the surrounding medium. Glycosylation occurs either on the amino terminal end of the protein, as with haemoglobin [2], or on the free amino group of lysine. Because of this glycosylation, the tertiairy or quaternary structure, function and/or degradation of the protein molecule may be altered, as has been demonstrated with glycosylated haemoglobin (HbA0 Fibrinogen is a protein with a half-life of 3-4 days, which occupies a central position in blood clotting. It is known that the e-amino groups of lysine in the fibrinogen molecule play an important role in cross-linking fibrin monomers and in fibrinolysis. We have therefore investigated whether glycosylation of fibrinogen is increased in the blood of diabetic patients. Subjects and methods SubjectsTwenty-two healthy volunteers (aged 21-59 years, mean 33 years; mean blood glucose level at the time of sampling, 5.1 _+ 1.0 mmol/1) and 26 Type 1 (insulin-dependent) diabetic patients (aged 19-57 years, mean 36 years; taking no medication other than insulin) participated in the study. MethodsBlood was collected in 3.2% sodium citrate (1 : 10, wt/vol) for purification of fibrinogen and estimation of glycosylation. After centrifugation at 5000 g for 20 min, plasma was either processed immediately or stored at -26~ Blood was also taken for estimation of glucose and HbAv HbA1 was estimated by the microcolumn method ([solab In-

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Section: Methodsmentioning

confidence: 99%

Glycosylation of human fibrinogen in vivo

et al. 1985

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“…Glycosylated hemoglobin (GHb) : was determined by method of Fluckiger et al (8). The red blood cells were thoroughly washed with saline and then hydrolyzed with oxalic acid (i.e.…”

Section: Reduced Glutathione (Gsh)mentioning

confidence: 99%

Antioxidant status in patients with acute myocardial infarction

Patil¹,

Chavan²,

Karnik³

2007

Indian J Clin Biochem

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“…There is no established reference method for determining the extent of non-enzymatic glycosylation of a protein. The most widely used chemical procedure is the thiobarbituric acid assay, originally developed for quantitation of haemoglobin glycosylation [74]. Careful standardization of the assay procedure is essential to obtain reproducible results [751.…”

Section: Current Assay Proceduresmentioning

confidence: 99%