ABSTRACT
Anaemia is a major health issue that has a wide global impact involving approximately 1/3rd of patients with anaemia. HbA1C levels are not influenced by blood glucose levels alone. Studies suggest that conditions like IDA, haemolytic anaemia, alcohol ingestion, pregnancy, blood loss, and uraemia may alter HbA1C levels independent of glycaemic status. Methods: Totally 200 patients were included in the study.. 100 patients were controlled diabetics with iron deficiency anemia and 100 were controlled diabetics without iron deficiency anemia. Comparison of levels of HbA1c was done between the two groups. Results: Correlation between mcv and hba1c is -0.76716. Which is strongly negative correlated. P – Value for the correlation test is 0.000001. Conclusion: Iron deficiency anemia has role in elevating A1C in both the groups. Iron deficiency anemia elevates HbA1c levels in diabetic individuals with controlled plasma glucose levels. The elevation is more in patients having plasma glucose levels between 100 to 126 mg/dl. Hence, before altering the treatment regimen for diabetes, iron deficiency anemia should be treated first.
ABSTRACT
Mn-peroxidase (MnP), a biotechnologically important enzyme was purified for the first time from a plant source Musa paradisiaca (banana) stem, which is an agro-waste easily available after harvest of banana fruits. MnP was earlier purified only from the fungal sources. The enzyme was purified from stem juice by ultrafiltration and anion-exchange column chromatography on diethylamino ethylcellulose with 8-fold purification and purification yield of 65%. The enzyme gave a single protein band in SDS-PAGE corresponding to molecular mass 43 kDa. The Native-PAGE of the enzyme also gave a single protein band, confirming the purity of the enzyme. The UV/VIS spectrum of the purified enzyme differed from the other heme peroxidases, as the Soret band was shifted towards lower wavelength and the enzyme had an intense absorption band around 250 nm. The Km values using MnSO4 and H2O2 as the substrates of the purified enzyme were 21.0 and 9.5 μM, respectively. The calculated kcat value of the purified enzyme using Mn(II) as the substrate in 50 mM lactate buffer (pH 4.5) at 25°C was 6.7s-1, giving a kcat/Km value of 0.32 μM-1s-1. The kcat value for the MnP-catalyzed reaction was found to be dependent of the Mn(III) chelator molecules malonate, lactate and oxalate, indicating that the enzyme oxidized chelated Mn(II) to Mn(III). The pH and temperature optima of the enzyme were 4.5 and 25°C, respectively. The enzyme in combination with H2O2 liberated bromine and iodine in presence of KBr and KI respectively. All these enzymatic characteristics were similar to those of fungal MnP. The enzyme has the potential as a green brominating and iodinating agent in combination with KBr/KI and H2O2.