Serum Proteins

Genetic polymorphisms of blood groups ABO and RH D, serum proteins HP, TF, and GC, and red cell enzymes ACP1, PGM1, ESD, GLO1, and SOD-A have been reported for three tribes (Torguts, Derbets, and Buzavs) of the Volga’s Kalmyk-Oyrats. The Kalmyks exhibit genetic markers that are characteristic of Central Asian populations, namely, high allelic frequencies for ABO*B, TF*C2, GC*1F, ESD*2, and GLO1*2, and the rare incidence of individuals with the RH-negative phenotype. Genetic distance measures reveal that close genetic affinities exist between the Derbets and Buzavs, but both populations differ significantly from the Torguts. Collectively as an ethnic group, the Kalmyks genetically resemble the contemporary Buryats of the Baikal region of southeastern Siberia and the Mongols of Mongolia. The transplantation of the Kalmyk-Oyrats from their homeland near Lake Baikal to their current residence (4500 km) near the Caspian Sea and their subsequent isolation for more than 300 years have not appreciably altered the gene frequencies from the parental populations for frequencies of standard genetic markers.

The powder protein is mostly used as the main dietary by bodybuilders for improving exercise training. This research studied the effect of the powder protein intake on serum total protein and creatinine concentrations, and urine pH and protein of three different groups. The serum total protein concentration has no relationship with the amount of powder protein intake and cannot be affected by it. But the serum creatinine concentration has a direct relationship with the amount of powder protein intake. The group A and B serum creatinine concentrations in their blood were abnormal due to lack in the amount of protein intake in their daily life and exercise. The group C used sufficient amounts of powder protein 1.2-1.4 gm/Kg/day, which maintained their creatinine concentration. This quantity of protein intake for bodybuilders is not only safe, but also is improved the training adaptations in their excises training. The urine tests indicated no significant differences (P < 0.01) between their pH and at the same time the trace amount of protein in some of individuals urine was observed.

Baseline haematology, blood chemistry and acute phase protein parameters have not previously been published for free-ranging eastern grey kangaroos (Macropus giganteus). Eight eastern grey kangaroos, including three adult males, three adult females and two subadult males from two different populations, were examined. Assays assessed the antibacterial activity of kangaroo serum against one Gram-positive and three Gram-negative bacteria. The kangaroo serum had a strong antibacterial response to Klebsiella pneumoniae, and moderate responses to Escherichia coli and Staphylococcus aureus. The presence and level of acute phase proteins, haptoglobin and serum amyloid A in kangaroos was investigated. Haptoglobin and serum amyloid A were present in kangaroo serum, but only haptoglobin was elevated in a kangaroo with capture myopathy and necrotic wounds. The findings of this study provide preliminary data on health parameters of free-ranging eastern grey kangaroos. These parameters can be used to assist in assessing health in free-ranging populations.

A multi-laboratory, simulator study investigated the wear of polytetrafluorethylene (PTFE) cups run in bovine serum. Each laboratory used its own test protocol with a variety of simulator types. Our wear model incorporated 32 mm dia CoCr heads matched to PTFE cups run with serum protein-concentrations in the range 17-69 mg/ml. The multi-lab data demonstrated that protein-concentration had the most significant effect on wear performance. Both inverted and anatomical cups followed the same trend with first a rapid increase in wear-rates apparent for the initially low-protein levels and then a wear-rate reduction effect becoming apparent beyond 17 mg/ml of proteins. The results showed that as the protein concentration increased from 17 to 69 mg/ml, the magnitude of the wear-rates increased 200% but the protein wear-rate gradient decreased 24-60% with "inverted" and "anatomical" cups, respectively. This effect was more pronounced with 'anatomical" than "inverted" cups. Thus, the wear-trends with "inverted" cups were generally the more consistent, particularly at the low-protein levels. Increasing the serum volume by two-fold in one study increased the PTFE wear-magnitudes approximately 40% and the protein-wear gradient by 30%. These PTFE wear phenomena were consistent with the concept that low-concentrations of proteins promoted polymer wear but high-protein concentrations resulted in a protein-degradation phenomenon which progressively masked the actual polymer wear. In the selected protein range 17-69 mg/l, the multi-laboratory simulator data consistently overestimated the average clinical wear-rate by at least 50-100% depending on protein range. It would, therefore, appear clinically relevant to study PTFE wear with an inverted-cup model using a large volume of serum but only in low-protein concentrations. The protein-related wear phenomena observed with PTFE cups in this multi-laboratory project may also have relevance for wear-simulation of UHMWPE cups.

The physico-chemical properties of nanoparticles (NPs), such as small dimensions, surface charge and surface functionalization, control their capability to interact with cells and, in particular, with sub-cellular components. This interaction can be also influenced by the adsorption of molecules present in biological fluids, like blood, on NP surface. Here, we analysed the effect of serum proteins on 49 and 100 nm red fluorescent polystyrene NP uptake in porcine aortic endothelial (PAE) cells, as a model for vascular transport. To this aim, NP uptake kinetic, endocytic pathway and intracellular trafficking were studied by monitoring NPs inside cells through confocal microscopy and multiple particle tracking (MPT). We demonstrated that NPs are rapidly internalized by cells in serum-free (SF) medium, according to a saturation kinetic. Conversely, in 10% foetal bovine serum-enriched (SE) medium, NP uptake rate results drastically reduced. Moreover, NP internalization depends on an active endocytic mechanism that does not involve clathrin-and caveolae-mediated vesicular transport, in both SE and SF media. Furthermore, MPT data indicate that NP intracellular trafficking is unaffected by protein presence. Indeed, approximately 50-60% of internalized NPs is characterized by a sub-diffusive behaviour, whereas the remaining fraction shows an active motion. These findings demonstrate that the unspecific protein adsorption on NP surface can affect cellular uptake in terms of internalization kinetics, but it is not effective in controlling active and cellular-mediated uptake mechanisms of NPs and their intracellular routes.