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Abnormal angiogenesis is associated with various diseases such as solid tumors and metastasis, retinopathies, and rheumatoid arthritis. VEGF-A is the most important mediator of angiogenesis among all growth factors. The bioactivity of VEGF is mediated by two tyrosine kinase receptors VEGFR-1 and VEGFR-2 present on endothelial cells. VEGF signaling through VEGFR-2 is the major angiogenic pathway that leads to stimulation of endothelial cell ingrowths into the tumor. It comprised of an extracellular portion, a cytoplasmic portion, and a short transmembrane domain. The extracellular portion consists of seven Ig-like domains (D1–D7), of which the 1st to 3rd domains function as ligand-binding sites. In the present work, a soluble recombinant extracellular domain 1-3 of VEGFR-2 was expressed in Pichia pastoris to inhibit the VEGF-induced angiogenesis. The 975 bp DNA fragment containing extracellular domain 1-3 kdr, was designed according to the nucleotide sequence at GenBank and protein sequence at Swiss-Prot. The recombinant secretory expression vector (pPinkαHC/KDR1-3) was constructed and transferred into yeast by electroporation. The high expression transformants were identified through complementation of adenine auxotrophy and cultured. KDR1-3 was expressed under the induction of %1 methanol and confirmed by using SDS-PAGE and western blot techniques. After being purified by affinity chromatography using Ni-NTA resins, binding of expressed product to hVEGF165 was proved by two direct ELISA and ELISA receptor binding assays. The data showed that human VEGFR-2 extracellular domain 1-3 with eukaryotic protein structure, that there is no reported paper about, was successfully expressed. 

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The presence of antibacterial activity in bovine β-lactoglobulin and in α-lactalbumin hydrolysates was investigated. The Plasmin-Digest of β-lactoglobulin (PDβ) and of α-lactalbumin (PDα) were fractionated, using reversed phase high performance liquid chromatography. The antibacterial activity of β-lactoglobulin, α-lactalbumin, nisin, plasmin, PDβ and PDα were in vitro tested against pathogenic (Escherichia coli and Staphylococcus aureus) and probiotic (Lactobacillus casei and Lactobacillus acidophilus) bacteria. Although α-lactalbumin, β-lactoglobulin and plasmin exhibited no antibacterial activity, PDβ, PDα and nisin revealed antibacterial activity against the bacteria tested. The Minimum Inhibitory Concentration (MIC) of these compounds was determined for the bacteria cultures. Similar to nisin, the MIC of PDβ and of PDα against Gram-positive bacteria was recorded as considerably lower than the MICs against Gram-negative bacteria. The study also evaluated the effect of PDβ, PDα and nisin on the growth curves and on the plate count confirmations of the target bacteria. The results revealed that nisin, PDβ and PDα have inhibitory effects on the lag phase, maximum OD620 and on plate count confirmation of the bacteria tested. The maximum inhibitory effect of these compounds was created during the log phase. Their inhibitory effects depended upon their concentrations, higher concentration causing stronger antibacterial activity. The PDβ and PDα proved more active against Gram-negative bacteria than did nisin, but nisin revealed substantial inhibitory activity against Gram-positive bacteria.