Actin

+ Khả năng kết hợp với actin - Myosin gắn với actin ở 2 trung tâm đặc hiệu  actomyosin. - Hoạt tính ATPase của actomyosin được cả Mg++ và Ca++ hoạt hoá (Khác với ATPase của myosin là Ca++ hoạt hoá và ion Mg++ ức chế). + Khả năng kết hợp với actin - Myosin gắn với actin ở 2 trung tâm đặc hiệu  actomyosin. - Hoạt tính ATPase của actomyosin được cả Mg++ và Ca++ hoạt hoá (Khác với ATPase của myosin là Ca++ hoạt hoá và ion Mg++ ức chế). ...

51p fpt_12 21-05-2013 94 13   Download

Đề tài ngiên cứu nhằm mô tả các hình thái lâm sàng và giải phẫu bệnh của ung thư ống tiêu hóa không thuộc biểu mô; mô tả các phương pháp phẫu thuật và đánh giá kết quả điều trị phẫu thuật của ung thư ống tiêu hóa không thuộc biểu mô. Mời các bạn cùng tham khảo nội dung chi tiết.

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Mục tiêu của đề tài là mô tả các hình thái lâm sàng và giải phẫu bệnh của ung thư ống tiêu hóa không thuộc biểu mô; mô tả các phương pháp phẫu thuật và đánh giá kết quả điều trị phẫu thuật của ung thư ống tiêu hóa không thuộc biểu mô. Mời các bạn cùng tham khảo nội dung chi tiết.

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Tham khảo Hoạt động của các sợi trong bộ xương tế bào để nằm vững các kiến thức về phân loại ống vi thể, sợi actin, sợi trung gian từ cấu tạo đến nhiệm vụ của từng loại.

9p vuhoablue 26-09-2014 148 21   Download

Đề tài được thực hiện nhằm phát triển và ứng dụng quy trình mPCR phát hiện đồng thời MBV và WSSV trên tôm sú (Penaeus monodon). Sau khi thực hiện quy trình mPCR của (Karlo et al., 2006) với mẫu dương tính với MBV cho kết quả ở vị trí 361bp. Sau đó tiếp tục phát triển quy trình mPCR phát hiện đồng thời MBV và gen β-actin cho kết quả hiện hai vạch ở vị trí 361bp (MBV) và 216 (β-actin).

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HOÀN THIỆN QUI TRÌNH PCR ĐA MỒI PHÁT HIỆN ĐỒNG THỜI VI RÚT GÂY BỆNH ĐỐM TRẮNG (White Spot Syndrome Virus) VÀ VI RÚT GÂY BỆNH CÒI (Monodon Baculovirus) Ở TÔM SÚ (Penaeus monodon) CÓ SỬ DỤNG GEN β-ACTIN LÀM NỘI CHUẨN

8p xanieu 01-07-2013 110 5   Download

UMR 5539 (CNRS) Laboratoire de Motilite Cellulaire (Ecole Pratique des Hautes Etudes), Universite de Montpellier, France; ´ Centre de Recherches de Biochimie Macromoleculaire, Montpellier, France; 3Genes and Development Group, Department of Biomedical Sciences, University of Edinburgh, Scotland It is generally assumed that of the six domains that comprise gelsolin, domain 2 is primarily responsible for the initial contact with the actin filament that will ultimately result in the filament being severed.

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The ¯uorescence resonance energy transfer parameter, f, is de®ned as the eciency of the energy transfer normalized by the quantum yield of the donor in the presence of acceptor. It is possible to characterize the ¯exibility of the protein matrix between the appropriate ¯uorescent probes by monitoring the temperature dependence of f. The intermonomer ¯exibility of the Ca-actin and Mg-actin ®laments was characterized by using this method at pH values of 6.5 and 7.4.

8p research12 01-06-2013 54 4   Download

Ikkai&Ooi [Ikkai,T.&Ooi,T. (1966)Biochemistry5, 1551± 1560] made a thorough study of the e€ect of pressure on G- and F-actins. However, all of the measurements in their study were made after the release of pressure. In the present experiment in situ observations were attempted by using eATP to obtain further detailed kinetic and thermodynamic information about the behaviour of actin under pressure.

8p research12 29-04-2013 41 7   Download

A marked pH-dependent interaction with F-actin is an important property of typical members of the actin depolymerizing factor (ADF)/cofilin family of abundant actin-binding proteins. ADF/cofilins tend to bind to F-actin with a ratio of 1 : 1 at pH values around 6.5, and to G-actin at pH 8.0. We have investigated the mechan-ism for the pH-sensitivity.

8p research12 23-04-2013 47 4   Download

Erythroid dematin is a major component of red blood cell junctional complexes that link the spectrin±actin cytoskel-eton to the overlying plasma membrane. Transcripts of dematinarewidelydistributed includinghumanbrain, heart, lung, skeletalmuscle, andkidney.Invitro, dematinbinds and bundles actin ®laments in a phosphorylation-dependent manner. The primary structure of dematin consists of a C-terminal domain homologous to theÔheadpieceÕ domain of villin, an actin-binding protein of the brush border cyto-skeleton. ...

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Mammalian tubulins and actins attain their native con-formation following interactions with CCT (the cytosolic chaperonin containing t-complex polypeptide 1). To study the b-tubulin folding in lower eukaryotes, an isotype of b-tubulin (b-T1) from the Antarctic ciliate Euplotes focardii, was expressed in Escherichia coli. Folding analysis was performed by incubation of the 35 S-labeled, denatured b-T1 in the presence, or absence, of purified rabbit CCT and cofactor A, a polypeptide that stabilizes folded monomericb-tubulin. ...

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The thermal unfoldingofmyosinsubfragment 1 (S1) cleaved by trypsin was studied by differential scanning calorimetry. In the absence of nucleotides, trypsin splits the S1 heavy chain into three fragments (25, 50, and 20 kDa). This cleavage has no appreciable influence on the thermal unfolding of S1 examined in the presence of ADP, in the ternary complexes of S1 with ADP and phosphate analogs, such as orthovanadate (Vi) or berylliumfluoride (BeFx), and in the presence of F-actin.

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Peptides corresponding to the N-terminus of skeletal myosin light chain 1 (rsMLC1 1–37) and the short loop of human cardiacb-myosin (hcM398–414) have been shown to interact with skeletal F-actin by NMR and fluorescence measurements. Skeletal tropomyosin strengthens the binding of the myosin peptides to actin but does not interact with the peptides. The binding of peptides cor-responding to the inhibitory region of cardiac troponin I (e.g. hcTnI128–153) to F-actin to form a 1 : 1 molar complex is also strengthened in the presence of tropomyo-sin. ...

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Gelsolin is a multidomain and multifunction protein that nucleates the assembly of filaments and severs them. The activation of gelsolin by calcium is a multistep process involving many calcium binding sites that act to unfold the molecule from a tight structure to a more loose form in which three actin-binding sites become exposed. Low pHis alsoknowntoactivategelsolin, in theabsenceof calciumand this too results in an unfolding of the molecule.

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The goal of this study was to relate conformational changes in the N-terminal domain of chicken troponin I (TnI) to Ca 2+ activation of the actin–myosin interaction.The two cysteine residues in this region (Cys48 and Cys64) were labeled with two sulfhydryl-reactive pyrene-containing fluorophores [N-(1-pyrene)maleimide, and N-(1-pyrene)-iodoacetamide].The labeled TnI showed a typical fluores-cence spectrum: two sharp peaks of monomer fluorescence and a broad peak of excimer fluorescence arising from the formation of an excited dimer (excimer)....

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The interaction of heat shock protein with molecular mass 25 kDa (HSP25) and its point mutants S77D + S81D (2D mutant) and S15D + S77D + S81D (3D mutant) with intact and thermally denatured actinwas analyzedbymeans of fluorescence spectroscopy and ultracentrifugation. Wild typeHSP25 did not affect the polymerization of intact actin. The HSP25 3D mutant decreased the initial rate without affecting the maximal extent of intact actin polymerization. G-actin heated at 40–45
C was partially denatured, but retained its ability to polymerize....

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BAP31 is a 28-kDa integral membrane protein of the endoplasmic reticulumwhose cytosolicdomaincontains two caspase recognition sites that are preferentially cleaved by initiator caspases,such as caspase-8. Recently,we reported that the caspase-resistant BAP31 inhibited Fas-mediated apoptotic membrane fragmentation and the release of cytochromec from mitochondria in KB epithelial cells (Nguyen M.,Breckenridge G.,Ducret A &Shore G. (2000) Mol. Cell.Biol.20,6731–6740).

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Gelsolin is an abundant calcium dependent actin filament severing and capping protein. In the absence of calcium the molecule is compact but in the presence of calcium, as its six similar domains alter their relativeposition, agenerallymore open configuration is adopted to reveal the three actin binding sites.

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Vertebrate troponin regulates muscle contraction through alternative bind-ing of the C-terminal region of the inhibitory subunit, troponin-I (TnI), to actin or troponin-C (TnC) in a Ca 2+ -dependent manner. To elucidate the molecular mechanisms of this regulation by molluskan troponin, we com-pared the functional properties of the recombinant fragments of Akazara scallop TnI and rabbit fast skeletal TnI.

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