GLORIA

GEOMAR Library Ocean Research Information Access

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
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 290 (1975), S. 35-47 
    ISSN: 1432-1912
    Keywords: Guinea Pig Atrial Muscle ; Ryanodine ; Ryanodine Steady-State Condition ; Post-Rest Potentiation ; Calcium Exchange
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of ryanodine and ryanodine steady-state condition (RSSC) on contractile-related calcium were examined in isolated guinea pig left atrial muscle. 1. RSSC is a specific irreversible condition occurring after a brief exposure to 1×10−7 M ryanodine, followed by washing. It is characterized by elimination of the contraction following a 10-sec rest interval (post-rest) and prolongation of the associated action potential duration (AP50%) from 78.9 to 160.8 msec with minimal alteration in steady-state tension development determined at 1 Hz. 2. Induction of RSSC with a ryanodine-bovine serum albumin conjugate produced similar alterations in post-rest contractile strength and action potential duration. 3. In the presence of 1×10−7 M ryanodine, guinea pig left atria exhibit a significant increase in total 45Ca efflux from two rapidly exchangeable compartments (compartment 1, t 1/2=1.58 min; compartment 2, t 1/2-8.20 min). 4. In atria loaded after the induction of RSSC, total 45Ca release was significantly reduced by 7.2% of the total exchange. 5. The 45Ca exchange space for RSSC atria was reduced from 23.22±0.81 to 19.85±1.22 ml per 100 g muscle without a significant reduction in the total exchange space. 6. From these results, it is concluded that the effects of low concentrations of ryanodine and RSSC are to alter the contractile calcium levels of the tissue, primarily from sarcolemmal membrane sites which regulate post-rest contractile strength and action potential duration.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 0948-5023
    Keywords: Keywords: Protein-Carbohydrate interactions ; MD simulations ; Flexibility ; Sialyllactose ; Influenza A virus hemagglutinin ; Murine polyoma virus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The attachment of a virus to the host cell surface is influenced by enthalpic and entropic factors. A detailed evaluation of all possible energetic interactions including the effects of solvent molecules seems to be a promising way to gain deeper insights in the overall process of binding. Here we performed intensive molecular dynamics studies to compare the conformational space available for the unbound sialyllactose in aqueous solution and when complexed with influenza A hemagglutinin and the murine polyoma virus. In general the conformational freedom of sialyllactose is considerably reduced compared to the free state. Remarkably, two different conformations of the Siaα(2-3)Galβ glycosidic linkages are preferred (which are both populated in the free state) when complexed with either protein.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...