Library

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 957 (1988), S. 340-344 
    ISSN: 0167-4838
    Keywords: CD ; Carboxamidomethylated RNAase A ; Guanidine ; RNAase A ; SDS ; Secondary structure
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Prostaglandins 47 (1994), S. 353-365 
    ISSN: 0090-6980
    Keywords: Ca current ; Prostaglandins ; patch clamp ; rat oarta ; smooth muscle cell ; vasodilation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 410 (1987), S. 385-393 
    ISSN: 1432-2013
    Keywords: Bovine aortic endothelial cells ; Patch clamp ; Inward rectifier ; Transient outward K current ; Ca current ; Endothelium-derived relaxing factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The electrophysiological properties of cultured bovine aortic endothelial cells were characterized using the patch clamp technique. Resting potentials were measured on passing to the whole cell recording configuration and were close to −65 mV in healthy cells. In cell-attached recordings with a high potassium pipette solution, inward single channel currents were observed with zero applied pipette potential. A linear slope conductance of 25 pS was found for a wide range of hyperpolarizing patch potentials and also for depolarizing patch potentials of up to 50–60 mV. A pronounced inward rectification was apparent as no reversal of these currents was seen for larger depolarizations. Whole cell recording in physiological solutions revealed the presence of a hyperpolarization-activated inward current with strong inward rectification and no voltage-dependent ionic current was observed upon depolarization in this subset of cells. Substitution of potassium for external sodium resulted in a shift in the zero current potential consistent with potassium being the main permeant ion. Together with the characteristic voltage-dependent blocking actions of external sodium ions and low concentrations of barium and caesium ions, our results indicate that this current is very similar to the classical inward rectifier as originally described in skeletal muscle and in tunicate eggs. In a second population of cells, a depolarization-activated outward current displaying characteristics of the fast transient A-type potassium current as first reported in molluscan neurones was also observed. No evidence for inward voltage dependent sodium or calcium currents was found.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1435-1536
    Keywords: Chymotrypsinogen ; chymotrypsin fragments ; CD ; secondary structure ; sodiumdodecylsulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Secondary structural changes of chymotrypsinogen A,α-chymotrypsin, and their isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245were examined in aqueous solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride (residue numbers from chymotrypsinogen). After the fragmentation by the cleavage of disulfide bridges inα-chymotrypsin, the helical structure was formed in the isolated polypeptide 16–146 where the helical segments do not exist in the protein state. The polypeptide 149–245, where the helical segments of the parent protein are originally located, contained no helices. The polypeptide 1–13 was almost disordered. The three polypeptides, chymotrypsinogen,α-chymotrypsin and the polypeptide 16–146, clearly showed differences in the stabilities of helical structures in solutions of urea and guanidine hydrochloride. The addition of SDS accelerated the formation of helical structures in each polypeptide except for 1–13.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...