scholarly journals Solid-phase refolding of poly-lysine tagged fusion protein of hEGF and angiogenin

2002 ◽  
Vol 7 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Sang Joong Park ◽  
Kang Ryu ◽  
Chang Woo Suh ◽  
Young Gyu Chai ◽  
Oh Byung Kwon ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Solid Phase

Differential expression of the ED sequence-containing form of cellular fibronectin in embryonic and adult human tissues

1987 ◽  
Vol 88 (4) ◽  
pp. 419-430
Author(s):  
T. Vartio ◽  
L. Laitinen ◽  
O. Narvanen ◽  
M. Cutolo ◽  
L.E. Thornell ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Antigenic Determinant ◽  
Solid Phase ◽  
Basement Membranes ◽  
Malignant Tumours ◽  
Embryonic Tissues ◽  
Adult Tissues ◽  
Decidual Cells ◽  
Foetal Kidney ◽  
Cellular Fibronectin

Monoclonal mouse hybridoma antibodies were obtained for secreted cellular fibronectin (cFn) from A8387 fibrosarcoma cells. One of them, 52-DH1 (DH), reacted exclusively with cFns but not with plasma Fns (pFns) in immunoblotting and solid-phase EIA. The DH antibody also recognized thermolysin cFn fragments and beta-galactosidase-Fn fusion protein which contained the ED sequence specific to at least some forms of cFns. On the other hand, the DH antibody failed to recognize a fusion protein that was otherwise identical but lacked the ED sequence. Thus, the antigenic determinant for the DH antibody was located to the ED sequence. The DH antibody was then used to study the expression of ED sequence containing cFn (EcFn). For comparisons, another monoclonal antibody, 52BF12 (BF), recognizing equally well both pFns and cFns, was used. Immunoblotting of pFn fragments indicated that this antibody had the antigenic determinant at or close to the cell-binding site of Fn. EcFn was revealed by the DH antibody in embryonic and adult fibroblasts and in a variety of other cultured normal and malignant human cells. In embryonic tissues EcFn was abundant in developing basement membranes, as shown in foetal kidney and muscle, while in adult tissues it was confined only to endothelia of larger blood vessels. Furthermore, in embryonic tissues the capillaries showed bright EcFn-positivity not found any more in adult tissues. Human plasma contained a small quantity of EcFn, which may hence have an endothelial origin. EcFn was also prominent in the stroma of malignant tumours as well as in reactive benign conditions, such as granulation tissue and decidual cells. The results suggest that EcFn is a form of the protein which may have a particular role in developing and reactive tissues in embryos and adults.

Covalent immobilization and solid-phase refolding of enterokinase for fusion protein cleavage

2005 ◽  
Vol 40 (5) ◽  
pp. 1755-1762 ◽  
Author(s):  
Chang Woo Suh ◽  
Sin Hye Park ◽  
Seung Gook Park ◽  
Eun Kyu Lee
Keyword(s):  
Fusion Protein ◽  
Solid Phase ◽  
Covalent Immobilization ◽  
Protein Cleavage ◽  
Fusion Protein Cleavage

Solid-phase synthesis and application of double-fluorescent-labeled lipopeptides, containing a CTL-epitope from the measles fusion protein

1999 ◽  
Vol 54 (5) ◽  
pp. 436-443 ◽  
Author(s):  
P. Hoogerhout ◽  
K.J. Stittelaar ◽  
H.F. Brugghe ◽  
J. A. M. Timmermans ◽  
G.J. Ten Hove ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Phase Synthesis ◽  
Ctl Epitope

scholarly journals The C-Terminal Portion of the Tail Fiber Protein of Bacteriophage Lambda Is Responsible for Binding to LamB, Its Receptor at the Surface of Escherichia coli K-12

2000 ◽  
Vol 182 (2) ◽  
pp. 508-512 ◽  
Author(s):  
Jiang Wang ◽  
Maurice Hofnung ◽  
Alain Charbit
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Solid Phase ◽  
Cell Surface Receptor ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Intact Cells ◽  
Fiber Protein ◽  
Surface Receptor ◽  
K 12

ABSTRACT Bacteriophage λ adsorbs to its Escherichia coli K-12 host by interacting with LamB, its cell-surface receptor. We fused C-terminal portions of J, the tail fiber protein of λ, to maltose-binding protein. Solid-phase binding assays demonstrated that a purified fusion protein comprising only the last 249 residues of J could bind to LamB trimers and inhibited recognition by anti-LamB antibodies. Electron microscopy further demonstrated that the fusion protein could also bind to LamB at the surface of intact cells. This interaction prevented λ adsorption but affected only partially maltose uptake.

Solid-phase binding assays of peptides using EGFP-Src SH2 domain fusion protein and biotinylated Src SH2 domain

2005 ◽  
Vol 15 (22) ◽  
pp. 4994-4997 ◽  
Author(s):  
Guofeng Ye ◽  
Marina Ayrapetov ◽  
Nguyen-Hai Nam ◽  
Gongqin Sun ◽  
Keykavous Parang
Keyword(s):  
Fusion Protein ◽  
Solid Phase ◽  
Sh2 Domain ◽  
Binding Assays ◽  
Domain Fusion ◽  
Solid Phase Binding

Solid-phase immunoelectron microscopy for rapid diagnosis of enteroviruses

1984 ◽  
Vol 42 ◽  
pp. 226-227 ◽  
Author(s):  
K. Pegg-Feige ◽  
F. W. Doane
Keyword(s):  
Electron Microscopy ◽  
Cell Culture ◽  
Immunoelectron Microscopy ◽  
Detection Method ◽  
Solid Phase ◽  
Protein A ◽  
Plant Viruses ◽  
Rapid Diagnosis ◽  
Virus Diagnosis ◽  
Antiviral Antibody

Immunoelectron microscopy (IEM) applied to rapid virus diagnosis offers a more sensitive detection method than direct electron microscopy (DEM), and can also be used to serotype viruses. One of several IEM techniques is that introduced by Derrick in 1972, in which antiviral antibody is attached to the support film of an EM specimen grid. Originally developed for plant viruses, it has recently been applied to several animal viruses, especially rotaviruses. We have investigated the use of this solid phase IEM technique (SPIEM) in detecting and identifying enteroviruses (in the form of crude cell culture isolates), and have compared it with a modified “SPIEM-SPA” method in which grids are coated with protein A from Staphylococcus aureus prior to exposure to antiserum.

Application of solid-phase immune electron microscopy to study physical and stability characteristics of enterically transmitted non-a, non-b hepatitis virus

1988 ◽  
Vol 46 ◽  
pp. 80-81
Author(s):  
Charles D. Humphrey ◽  
E. H. Cook ◽  
Karen A. McCaustland ◽  
Daniel W. Bradley
Keyword(s):  
Electron Microscopy ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Solid Phase ◽  
Etiologic Agent ◽  
World Health ◽  
Health Concern ◽  
Morphological Identification ◽  
Immune Electron Microscopy

Enterically transmitted non-A, non-B hepatitis (ET-NANBH) is a type of hepatitis which is increasingly becoming a significant world health concern. As with hepatitis A virus (HAV), spread is by the fecal-oral mode of transmission. Until recently, the etiologic agent had not been isolated and identified. We have succeeded in the isolation and preliminary characterization of this virus and demonstrating that this agent can cause hepatic disease and seroconversion in experimental primates. Our characterization of this virus was facilitated by immune (IEM) and solid phase immune electron microscopic (SPIEM) methodologies.Many immune electron microscopy methodologies have been used for morphological identification and characterization of viruses. We have previously reported a highly effective solid phase immune electron microscopy procedure which facilitated identification of hepatitis A virus (HAV) in crude cell culture extracts. More recently we have reported utilization of the method for identification of an etiologic agent responsible for (ET-NANBH).

Identification of hepatitis a virus in cell cultures by solid phase immune electron microscopy

1986 ◽  
Vol 44 ◽  
pp. 238-239
Author(s):  
C.D. Humphrey ◽  
T.L. Cromeans ◽  
E.H. Cook ◽  
D.W. Bradley
Keyword(s):  
Electron Microscopy ◽  
Liquid Phase ◽  
Cell Cultures ◽  
Rapid Detection ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Solid Phase ◽  
Immune Electron Microscopy ◽  
Detection And Identification

There is a variety of methods available for the rapid detection and identification of viruses by electron microscopy as described in several reviews. The predominant techniques are classified as direct electron microscopy (DEM), immune electron microscopy (IEM), liquid phase immune electron microscopy (LPIEM) and solid phase immune electron microscopy (SPIEM). Each technique has inherent strengths and weaknesses. However, in recent years, the most progress for identifying viruses has been realized by the utilization of SPIEM.

Dynamic studies of silicide-mediated crystallization of amorphous silicon

1992 ◽  
Vol 50 (2) ◽  
pp. 1352-1353
Author(s):  
C. Hayzelden ◽  
J. L. Batstone
Keyword(s):  
Ion Implantation ◽  
Solid Phase ◽  
Metallic Phase ◽  
Single Crystal Substrate ◽  
Free Electrons ◽  
Melt Temperature ◽  
Transmission Electron ◽  
Crystal Substrate ◽  
High Resolution Tem

Epitaxial reordering of amorphous Si(a-Si) on an underlying single-crystal substrate occurs well below the melt temperature by the process of solid phase epitaxial growth (SPEG). Growth of crystalline Si(c-Si) is known to be enhanced by the presence of small amounts of a metallic phase, presumably due to an interaction of the free electrons of the metal with the covalent Si bonds near the growing interface. Ion implantation of Ni was shown to lower the crystallization temperature of an a-Si thin film by approximately 200°C. Using in situ transmission electron microscopy (TEM), precipitates of NiSi2 formed within the a-Si film during annealing, were observed to migrate, leaving a trail of epitaxial c-Si. High resolution TEM revealed an epitaxial NiSi2/Si(l11) interface which was Type A. We discuss here the enhanced nucleation of c-Si and subsequent silicide-mediated SPEG of Ni-implanted a-Si.Thin films of a-Si, 950 Å thick, were deposited onto Si(100) wafers capped with 1000Å of a-SiO2. Ion implantation produced sharply peaked Ni concentrations of 4×l020 and 2×l021 ions cm−3, in the center of the films.

TEM characterization of Au/Polysilicon interactions

1990 ◽  
Vol 48 (4) ◽  
pp. 650-651
Author(s):  
N. David Theodore ◽  
Leslie H. Allen ◽  
C. Barry Carter ◽  
James W. Mayer
Keyword(s):  
Solid Phase ◽  
Single Crystal Silicon ◽  
Chemical Vapor ◽  
Electrical Contacts ◽  
Silicon Substrates ◽  
Crystal Silicon ◽  
Transmission Electron ◽  
Polysilicon Films ◽  
The Stability

Metal/polysilicon investigations contribute to an understanding of issues relevant to the stability of electrical contacts in semiconductor devices. These investigations also contribute to an understanding of Si lateral solid-phase epitactic growth. Metals such as Au, Al and Ag form eutectics with Si. reactions in these metal/polysilicon systems lead to the formation of large-grain silicon. Of these systems, the Al/polysilicon system has been most extensively studied. In this study, the behavior upon thermal annealing of Au/polysilicon bilayers is investigated using cross-section transmission electron microscopy (XTEM). The unique feature of this system is that silicon grain-growth occurs at particularly low temperatures ∽300°C).Gold/polysilicon bilayers were fabricated on thermally oxidized single-crystal silicon substrates. Lowpressure chemical vapor deposition (LPCVD) at 620°C was used to obtain 100 to 400 nm polysilicon films. The surface of the polysilicon was cleaned with a buffered hydrofluoric acid solution. Gold was then thermally evaporated onto the samples.

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