Changes in molecular size and shape of hemoglobin of systemic lupus erythermatosus

Different hemoglobin derivatives concentration and electrical conductivity were measured for patients suffered from, in addition the dielectric relaxation in the frequency range 100 KHz up to 10 MHz of Hb molecule of systemic lupus patients compared to normal control. Abnormal dynamic motion of Hb was found, a lack of changes in the size and/or shape of Hb. Also, the dielectric results indicating that the molecular shape tends to deviate from the spherical form as the activity [severity] of the disease increases

In vivo effect of [50Hz] magnetic Filed on concentration of trace elements concerned with hemoglobin formation

The present in vivo experiment was designed to establish whether the exposure to 50 Hz magnetic field induces changes in blood and organs store of trace elements concentrations possibly associated with changes in hemoglobin level and induction of anemia. Rats were exposed to a high magnetic field strength of 0.5 T for one hour daily, the experiment was conducted for 30 days. Thirty-six rats were divided into control and magnetic field exposed rats. Iron, copper and zinc concentrations in blood, liver, kidney and spleen were estimated to assess the magnetic field effect on trace element storage in these tissues. MF exposure resulted in a depletion of the organs store of trace elements. A highly significant increase in blood copper and a decrease in zinc and iron levels were detected. A significant decrease was found in the hematological parameters, ceruloplasmin and ferritin [iron metabolism parameters]. The changes observed were associated with anemia during the first 14 days of MF exposure. The magnitude of anemia increased with increasing the exposure time

Molecular study of proteoglycans in rheumatoid

In this study, ten samples of synovial fluid were aspirated from normal as well as another ten rheumatoid samples. Proteoglycans were extracted from synovial fluids, then purified by gel chromatography. The results showed that there was an alteration in the structure of rheumatoid arthritic proteoglycans. The molecular weight was lower in rheumatoid proteoglycans as shown from the elution volume of the isolated proteoglycans. A shift and a decrement in the absorbance peak of proteoglycans absorption spectrum were observed. Moreover, there was an alteration in the bands number of high voltage electrophoresis. Fractions separated from normal and rheumatoid proteoglycans had the same number, but they were different in contents. Furthermore, a significant difference in amino acid contents between the two groups was detected, this alteration was suggested to be due to either the enzymatic activity or the alteration in m-RNA