الفهرس 
TYPE 1 DIABETESOnly 14 pages are availabe for public view
 |  | from | 137 |  |  |
| | | from | 137 | | |
Abstract
T
his study was a cross – sectional case control study designed to assess the oxygen-binding characteristics of children and adolescents with type 1 diabetes by determination of position and intensity of Raman scattering (RS) bands of haemoglobin spectrum depend on variations of links in a porphyrin ring that allowing estimatation of the conformational changes of haematoporphyrin.
The study included 35 patients with type 1 DM recruited from the Pediatric Diabetes Clinic, Children’s hospital, Ain Shams University. They were 22 (62.9%) female &13 (37.1%) male. cases were compared with thirty five age & sex apparently healthy subjects.
The character of spectra in Raman scattering (RS) of hemoglobin allows us to determine the degree of oxidation of the iron atom included, its spin state, and the presence of ligands and reflects changes in the structure of globin, leading to deformation of hemoprotein and affecting oxygen binding properties of hemoglobin.
Date from the current study showed that he value of symmetric and asymmetric fluctuations of pyrrol rings (I1375/I1172) increased in patient with DM than control. The ability of Hb to bind 02 (I1355/I1550) decreased in patient with DM than control. Additionally, the ability of Hb to bind 02 decreased with high (HbA1C, lipid profile, duration of disease, total daily dose) and micro albuminuria.
The affinity of Hb to 02 (I1355/I1550)/ (I1375/I1580) decreased in patients. Furthermore, affinity of Hb to 02 decreased with high (HbA1C, lipid profile, duration of disease, total daily dose) and micro albuminuria. The relative amount of 0-Hb in blood I1375/(I1355+I1375) increased in patients.
Bohr’s effect provides explanation for this Hb changes in erythrocyte, the molecular mechanism of Bohr’s effect is studied on human Hb. According to the two-state allosteric model, Hb exists in equilibrium between two different conformations, which differ in their internal affinity to oxygen: tense (T-form) and relaxed (R-form). The dominant mechanism of transition between Hb’s R- and T-forms lies in the movement of the iron atom into or away from the region of the porphyrin ring.