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Rheumatoid arthritis (RA) is an autoimmune disorder of the joints that is characterized by extra-articular involvement in addition to inflammatory arthritis. Joint and periarticular tissue loss brought on by inflammation results in functional impairment. To lessen the significant daily challenges that patients confront and to ensure better outcomes, early detection and treatment are essential. The study's objective was to establish the use of human β-defensin-2 (HBD-2) as a RA diagnostic marker. A total of 60 RA patients and 30 healthy controls participated in the research. The ELISA technique was used to measure serum HBD-2. The following tests were performed: complete blood count (CBC), erythrocyte sedimentation rate (ESR), renal function test, and liver function test. In comparison to the healthy control group, the RA group exhibited a substantially higher blood HBD-2 levels (p ≤0.001). Additionally, there was no significant association between serum HBD-2 and urea, creatinine, AST, ALT, and ESR (P>0.05). When RA was distinguished from the group of healthy individuals, the area under the curve (AUC) demonstrated excellent diagnostic accuracy (AUC = 0.990, p = 0.001). (0.9667). As a result, serum HBD-2 may be used as a reliable RA diagnostic marker.

According to the high operational costs, low stability, and reusability of enzymes, immobilization by nanoparticle gathering has increased in recent years. Iron oxide nanoparticles (magnetite nanoparticles, Fe₃O₄) have been prepared by mixing one volume of iron dioxide ions and two volumes of iron trioxide ions with HCl via the precipitation of iron salts by NH₄OH. The features of magnetic nanoparticles have been studied by Atomic Force Microscopy (AFM), X-Ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy, and Scanning Electron Microscopy (SEM). The prepared Fe3O4 was used in the adsorption method to immobilize the galactosidase enzyme. The immobilized enzyme has been compared with the crude one by optimizing time, PH, temperature, substrate solution concentration, and enzyme solution concentration. As a result, the immobilized enzyme has exhibited higher activity over long storage times, and a wide PH and temperature range than crude enzyme. In addition, whatever the substrate and enzyme concentrations, the activity of the immobilized enzyme increased over the non-immobilized one. As a result, a lower Km value for immobilized D-galactosidase indicates a higher affinity for the substrate than crude D-galactosidase.