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Example sentences for: aac
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The primer pair for β-actin was GTC CTC TCC CAA GTC CAC ACA (forward) and CTG GTC TCA AGT CAG TGT ACA GGT AA (reverse), that of IL-8 was CTG CGC CAA CAC AGA AAT TA (forward) and ATT GCA TCT GGC AAC CCT AC (reverse), that of MCP-1 was GCC TCC AGC ATG AAA GTC TC (forward) and TAA AAC AGG GTG TCT GGG GA (reverse), that of IP-10 was CCA CGT GTT GAG ATC ATT GC (forward) and TGG AAG ATG GGA AAG GTG AG (reverse), that of RANTES was CGC TGT CAT CCT CAT TGC TA (forward) and GCT GTC TCG AAC TCC TGA CC (reverse), that of MIP-1α was TGC AAC CAG TTC TCT GCA TC (forward) and ACA GGG GAA CTC TCA GAG CA (reverse), and that of MIP-1β was CTG GGT CCA GGA GTA CGT GT (forward) and ACA GTG GAC CAT CCC CAT AG (reverse).
Each of the megaprimers was purified and subsequently amplified with GL1 primer (5' TGT ATC TTA TGG TAC TGT AAC TG 3'), using StuI B or HincII B plasmid as a template.
1: GAT C TC GAT CCC GCG AAA TTA ATA CCA CTC ACT ATA GGG GAA TTG TGA GCG GAT AAC AAT TCC CCT (BglII site in bold)
The HCMV DNA was detected using HCMV1 (5' cct agt gtg gat gac cta cgg gcc a) and HCMV2 (5' cag aca cag tgt cct ccc gct cct c) primers producing 249 bp long amplicon and the DNA of HHV6 was amplified with specific primer pair HP0 (5' ccg caa tcg aat cca cct agc gg) and HP4 (5' gtg aga acg gat tcg aac agt gct g) yielding 440 bp product [ 23 24 ] . All amplifications were carried out with 20 pmol of each primer in 2 mM solution of MgCl 2 , 2 U of Tag Special DNA polymerase (Biovendor, Czech Republic), 0.3 mM of each dNTPs, 10× reaction buffer and 1 μg of isolated DNA according to the following conditions: 96°C for 4 min, (94°C for 10 sec, 58°C for 10 sec, 72°C for 20 sec) 36 times, and final extension at 72°C for 2 min.
The residues in the MIDAS motifs lie on three closely apposed loops located on the upper edge of the β-sheet, where they form the metal-binding site, with oxygen atoms in the aspartate, serine and threonine residues coordinating the metal ion [ 9 ] . In integrin α2β1, which is a collagen receptor, the metal-binding site also binds the collagen ligand through the conserved glutamate in a GFOGER motif (O = hydroxyproline) completing the coordination sphere of the metal [ 28 ] . In vivo, the binding of collagen at this site appears to be regulated through a conformational shift in which the loops forming the MIDAS site change from a closed to an open conformation [ 29 30 31 ] . Other proteins containing a domain with all three MIDAS motifs include the D-subunit of magnesium chelatase [ 32 ] , Ca-activated chloride-channel protein [ 33 34 ] , nitrate reductase (accession AAC79447), and the D subunit of nitric oxide reductase (accession AAC45374).
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