نتایج جستجو برای: histidine rich protein ii
تعداد نتایج: 1864136 فیلتر نتایج به سال:
23 Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally 24 used method for determining approximate molecular weight (MW) in protein research. 25 Migration of protein that does not correlate with formula MW, termed " gel shifting " appears 26 to be common for histidine-rich proteins but not yet studied in detail. We investigated " gel 27
Histidine-rich glycoprotein (HRGP) is an abundant heparin-binding plasma protein that efficiently arrests growth and vascularization of mouse tumor models. We have shown that the antiangiogenic effect of HRGP is dependent on its histidine/proline-rich domain, which needs to be released from the mother protein to exert its effects. Here we identify a 35-amino-acid peptide, HRGP330, derived from ...
Abstract Background: The cysteine rich region II of Plasmodium vivax Duffy Binding Protein (PvDBP-II) is essential during merozoite invasion into the human erythrocyte and because of this biological importance, PvDBP-II is a vaccine candidate and a target for protective immunity against vivax malaria. In the present study we improved the yield of this protein by using E. coli (M15/BL21) expr...
Microplusin, a Rhipicephalus (Boophilus) microplus antimicrobial peptide (AMP) is the first fully characterized member of a new family of cysteine-rich AMPs with histidine-rich regions at the N and C termini. In the tick, microplusin belongs to the arsenal of innate defense molecules active against bacteria and fungi. Here we describe the NMR solution structure of microplusin and demonstrate th...
The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a functionally important hydrogen bonding interaction.
In this issue of Blood, MacQarrie and colleagues show that histidine-rich glycoprotein (a negative acute-phase reactant), inhibits activated factor XII, a clotting protein implicated in inflammation and thrombosis.1 O f the 2 mechanisms for triggering blood clotting, only the tissue factor pathway is essential for normal hemostasis. The other— the contact pathway—appears to have no hemostatic r...
The structure and orientation of adsorbed myoglobin as directed by metal-histidine complexation at the liquid-film interface was studied as a function of time using neutron and X-ray reflectivity (NR and XR, respectively). In this system, adsorption is due to the interaction between iminodiacetate (IDA)-chelated divalent metal ions Ni(II) and Cu(II) and histidine moieties at the outer surface o...
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