fastfit program (Fisons Instruments Inc)
90
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Fisons Instruments Inc
fastfit program
Fastfit Program, supplied by Fisons Instruments Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fastfit+program/fastfit+program/pm17548134-77-5-7
Average 90 stars, based on 1 article reviews
Fastfit Program, supplied by Fisons Instruments Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fastfit+program/fastfit+program/pm17548134-77-5-7
Average 90 stars, based on 1 article reviews
fastfit program - by Bioz Stars,
2026-10
90/100 stars
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other:Article Title: Optical biosensor study of ternary complex formation in a cytochrome P4502B4 system. Article Snippet: t o o The optical biosensor method was used for the revlation of ternary complexes, formed by the full-length ADPH–cytochrome P450 reductase (d-Fp) and cytohromes P4502B4 (d-2B4) and b5 (d-b5) in the course of heir interactions within the reconstituted d-2B4ontaining system.. Based on the lack of competition etween d-b5 and d-Fp for the binding sites on immoilized 2B4 (3) as well as on the analysis of data obained in the three proteins’ dissociation reactions, he possibility of formation of ternary complexes hrough the interactions between membranous hydrohobic fragments of proteins was substantiated.. All he complexes obtained were productive. Article Title: Molecular recognition in the p450cam monooxygenase system: direct monitoring of protein-protein interactions by using optical biosensor. Article Snippet: d A real-time optical biosensor study on the interactions between putidaredoxin reductase (PdR), putidaredoxin (Pd), and cytochrome P450cam (P450cam) within the P450cam system was conducted.. The binary Pd/P450cam and Pd/PdR complexes were revealed and kinetically characterized.. The dominant role of electrostatic interactions in formation of productive electron transfer complexes was demonstrated. Article Title: Optical biosensor investigation of interactions of biomembrane and water-soluble cytochromes P450 and their redox partners with covalently immobilized phosphatidylethanolamine layers. Article Snippet: A phospholipid-containing biochip was created by covalently immobilizing phospholipids on the optical biosensor’s aminosilane cuvette and employed to monitor the interactions of the membrane and watersoluble proteins in cytochrome P450-containing monooxygenase systems with planary layers of dilauroylphosphatidylethanolamine (DLPE) and distearoylphosphatidylethanolamine (DSPE), differing in acyl chain length.. It was shown that the full-length membrane proteins—cytochrome P4502B4 (d-2B4), cytochrome b5 (d-b5) and NADPH-cytochrome P450 reductase (d-Fp)—readily incorporated into the phospholipids.. The incorporation was largely due to hydrophobic interactions of membranous protein fragments with the phospholipid layer. Article Title: Immunogenicity and in vitro protective efficacy of a polyepitope Plasmodium falciparum candidate vaccine constructed by epitope shuffling. Article Snippet: A polyepitope chimeric antigen incorporating multiple protective and conservative epitopes from multiple antigens of Plasmodium faliparum has been considered to be more effective in inducing multiple layers of immunity against malaria than a single stageor single ntigen-based vaccine.. By modifying the molecular breeding approach to epitope shuffling, we have constructed a polyepitope chimeric gene hat encodes 11 B-cell and T-cell proliferative epitope peptides derived from eight key antigens mostly in the blood stage of Plasmodium alciparum.. A 35-kDa antigen encoded by this gene, named Malaria RCAg-1, was purified from an E. coli expression system. Article Title: The optical biosensor studies on the role of hydrophobic tails of NADPH-cytochrome P450 reductase and cytochromes P450 2B4 and b5 upon productive complex formation within a monomeric reconstituted system. Article Snippet: c c M The optical biosensor study of interaction between icrosomal proteins—NADPH-cytochrome P450 reuctase, cytochrome P450 2B4, and cytochrome b5— as carried out in the monomeric reconstituted sysem in the absence of phospholipids.. The formation of ndividual complexes was kinetically characterized nd their association and dissociation rate constants ere determined.. The association rate constants for he complexes formed were found to be close to the iffusiion limit—(0.5–4) 3 10 M s—while their disociation rate constants did not exceed 0.5 s. It was hown that the interprotein electron transfer can ocur both through complex formation and due to ranom collision. |