Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles: DFG German National Licenses  (2)
  • ELISA  (1)
  • Interfacial polycondensation  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Arrangement of MP26 in lens junctional membranes: Analysis with proteases and antibodies (1983)
    Springer
    The journal of membrane biology 74 (1983), S. 217-228 
    Details
    ISSN: 1432-1424
    Keywords: membrane topography ; ELISA ; electrophoretic transfer ; calf lens ; gap junctions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The major membrane protein of the bovine lens fiber cell is a 26-kilodalton (kD) protein (MP26), which appears to be a component of the extensive junctional specializations found in these cells. To examine the arrangement of MP26 within the junctional membranes, various proteases were incubated with fiber cell membranes that had been isolated with or without urea and/or detergents. These membranes were analyzed with electron microscopy and SDS-PAGE to determine whether the junctional specializations or the proteins were altered by proteolysis. Microscopy revealed no obvious structural changes. Electrophoresis showed that chymotrypsin, papain, and trypsin degraded MP26 to 21–22 kD species. A variety of protease treatments, including overnight digestions, failed to generate additional proteolysis. Regions on MP26 which were sensitive to these three proteases overlapped. Smaller peptides were cleaved from MP26 with V8 protease and carboxypptidases A and B. Protein domains cleaved by these proteases also overlapped with regions sensitive to chymotrypsin, papain, and trypsin. Specific inhibition of the carboxypeptidases suggested that cleavage obtained with these preparations was not likely due to contaminating endoproteases. Since antibodies are not thought to readily penetrate the 2–3 nm extracellular gap in the fiber cell junctions, antibodies to MP26 were used to analyze the location of the protease-sensitive domains. Antisera were applied to control (26 kD) and proteolyzed (22 kD) membranes, with binding being evaluated by means of ELISA reactions on intact membranes. Antibody labeling was also done following SDS-PAGE and transfer to derivatized paper. Both assays showed a significant decrease in binding following proteolysis, with the 22 kD product showing no reaction with the anti-MP26 sera. These investigations suggest that MP26 is arranged with approximately fourfifths of the primary sequence “protected” by the lipid bilayer and the narrow extracellular gap. One-fifth of the molecule, including the C-terminus, appears to be exposed on the cytoplasmic side of the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02332125
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Drug Transport Across Nylon 610 Films: Influence of Synthesis Variables (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 248-256 
    Details
    ISSN: 1573-904X
    Keywords: Nylon 610 ; Film ; Interfacial polycondensation ; Polymer ; Permeability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Nylon 610 is a hydrophilic polymer with considerable potential as a membrane for drug microencapsulation. To better understand drug transport through such membranes, the influence of the solvents and monomers used in the synthesis of nylon films were examined using a full factorial study. Nylon 610 films were synthesized by an interfacial polycondensation reaction using hexamethylenediamine (HD) in the water phase and sebacoyl chloride (SC) in the organic phase, which was a solvent blend of chloroform and trichlorotrifluoroethane at ratios of 1:1, 1:4, and 4:1. Monomer concentrations studied were 0.2, 0.4, and 0.6 M with respect to their appropriate phase, while the monomer ratios were 1:1, 3:1, and 1:3. The molecular weight, porosity, thickness, and crystallinity of the films were characterized. The transport of potassium chloride, hydrocortisone, and m-cresol was studied at 25°C as a function of the syntheses variables. Potassium chloride was selected to measure the porosity of the membrane. Hydrocortisone and m-cresol, a known solvent for nylon 610, were used to study pore and solution-diffusion transport, respectively. The molecular weight of the films was proportional to the chloroform concentration. As the molecular weight increased, film thickness, porosity, and hydrocortisone permeability increased. As the molecular weight decreased, film thickness and porosity decreased, while m-cresol permeability increased. These results can be explained on the basis of HD ability to readily partition into a good solvent such as chloroform permitting high molecular weight polymer to form before precipitation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016235111210
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...