ABSTRACT
INTRODUCTION: Deforming arthrosis, or osteoarthritis, is the most common rheumatic disease that involves the musculoskeletal system. The purpose of this research is to perform a retrospective review of the quality of life of patients with knee arthrosis, who underwent total knee arthroplasty (TKA) no less than 5 years ago, to evaluate, based on the Knee Society Scoring System, the efficacy of a modified measured resection technique, and to investigate factors that affect the outcomes. MATERIAL AND METHODS: The research sample consisted of 44 patients who had severe osteoarthrosis, Kellgren-Lawrence grade III and grade IV. RESULTS: The post-operative complications occurred in seven knee joints. Among them there were 2 cases of infection, 2 cases of periprosthesis fracture, and 2 cases of aseptic instability, each pair accounting for 4.3%, and 1 case of femoropatellar pain (2.3%). The remaining 38 knee joints (84.8%) were free of complications. CONCLUSIONS: Knee arthrosis is a serious health problem, given the significant rate of disability among patients and the significant reduction in the quality of life. Patients often seek medical help at the later stages of the disease, when pain is strong and knee function is significantly reduced. The approach to rehabilitation procedures and, in some cases, to lifestyle improvement should be more responsible.
ABSTRACT
The thermodynamic parameters for the protein-ligand binding have been obtained by microcalorimetry on three albumin samples (fatty acid free human serum albumin (I), fraction V human serum albumin (II), and fraction V bovine serum albumin (III)) bound with l-tryptophan (A) and three-ring tryptophan analogs (B and B*). The percentage, mu, of binding molecules (equivalent to the number of sites) is found to be 1.0 for I and 0.65 for II (in good agreement with dialysis results on the same systems) and 1.0 for III. The large negative delta H(bind) (-27.2 to -33.2 kJ . mol-1) constitutes the main contribution to delta G(bind) (-23.0 to -31.2 kJ . mol-1). The better binding of I-III towards B and B* compared with A is due to delta S(bind) being less negative. This is interpreted as a lesser loss of entropy for the three-ring ligands than for the normal tryptophan when they are bound. Data obtained on the proteins (heat of dilution; Huggins' constant, k') correlate well with mu or Qmax. This indicates that these physicochemical data could be used to characterize and compare rapidly some albumins of different sources. The unexpected finding that the parameters of I and III are nearer to each other than they are from II is discussed.
