The blot was hybridized with a radiolabeled EhCaBP2 coding region probe as described under " Experimental Procedures. 30 g of purified total RNA was separated in a 1.2% denaturing formaldehyde agarose gel and transferred onto a nylon membrane. Panel B, Northern blot analysis of EhCaBP2. Lane 1, EhCaBP2 plasmid DNA lane 2, EhCaBP1 plasmid DNA lane 3, total HM1:IMSS RNA and lane 4, same as lane 3 except no reverse transcriptase was added. The PCR products were electrophoresed in 1.2% agarose gel at 4 V/cm. The specificity of the primers for EhCaBP2 was checked by PCR amplification of Eh- CaBP1 and EhCaBP2-containing plasmid templates. The positions of the calcium binding domains are marked I-IV in this scheme. The location of the primers is indicated with arrows at the top of the figure. Panel A, amplification of EhCaBP2 RNA by RT-PCR. histolytica calcium-binding proteins involved in a novel calcium signal transduction pathway.Įxpression of EhCaBP2 RNA in E.
Our data suggest that EhCaBP2 is a new member ofĪ class of E.
In addition, a 12-mer peptide was identified fromĪ random peptide library that could differentially bind the two proteins. Activation of endogenous kinase was also found to be unique for the two proteins and the Ca2+ concentration required for their optimal functionality was also different. histolytica proteins in a Ca2+-dependent manner. Of studies indicated that EhCaBP1 and EhCaBP2 are functionally different. Homology-based structural modeling showed that the majorĭifferences between the two EhCaBPs lie in the central linker region, normally involved in binding target molecules. histolytica genome sequence data suggested that the two genes are non-allelic. Both of these genes are single copy, as revealed by Southern hybridization. Region between the second and third Ca2+ binding domains. This identity dropped to 40% in the 75-nucleotide central linker Comparison between the two genes showedĪn overall identity of 79% at the nucleotide sequence level. The two isoforms are encoded by genes of the same size (402 bp). Both EhCaBPs haveįour canonical EF-hand Ca2+ binding domains. Here, we report the identification and partial characterization of an isoform of this protein, EhCaBP2. We had previously characterized a novel calcium-binding protein (EhCaBP1) from E.
However, the mechanistic role of Ca2+ and calcium-binding proteins in the pathogenesis of E. Calcium plays a pivotal role in the pathogenesis of amebiasisīy modulating the cytopathic properties of the parasite. Lastly, we all know this the affordable “nano” version of the EMS Synthi Hi Fli…the apex vintage effect processor designed by David Cockerell, the effect and electronic engineer genius that wowed Mike Mathews back in the day(Frankfurt Trade show 1973), and who he subsequently hired as his top designer for EH, who was responsible for many of their best offerings.Entamoeba histolytica, an early branching eukaryote, is the etiologic agent of amebiasis. It is exceptionally clean…this rare transitional all black(no lines)very short lived version has the perfect combination of rarity/collectibility, AND being superior sounding.
Please check the many hi res photos as they form part of the description. Makes it very easy to play and conjure up unreal fat analog synth tones that the later reissues and current issues miss. This one is VERY responsive and has quick and accurate triggering especially on the shorter decay settings. It’s as fat sounding as any bass version I’ve had, and to my ears sounds closer to the 1st issue versions, but, with better triggering. I’ve had many of these over the years and this is among the best I’ve encountered alongside the first issue. Works 100%, all functions, no mods, all sliders functions perfectly, no noise or stickiness. For your consideration is a rare transitional early 2nd issue EH MICROSYNTH in excellent condition(easy 9/10) in original box.
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