English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

An abstract of the thesis of Steffen Koehler for the Master of Science in Physics presented July 6, 1995. Title: 0-Phthalaldehyde Modification of Sarcoplasmic Reticulum Calcium Release Muscle contraction is a phenomena which fascinated already the ancient Greeks. People have long sought to understand the mechanism of muscle contraction. Today we know that in order for muscle to contract, an action potential propagates from the nerve cell to the muscle cell. Upon arriving at the muscle cell, via a mechanism called ExcitationContraction (E-C) coupling, Ca+ is released from an intracellular membrane system, the sarcoplasmic reticulum (SR), into the intracellular fluid. The increase of intracellular Ca+ initiates the interaction between the contractile units which results in force development and tension. The least well understood step in the contractile process is mechanism of E-C coupling. During the last 15-20 years various theories have been proposed to describe this process. Our laboratory came up with a theory several years ago, that critical sultbydryl groups on a protein, the ryanodine receptor(RyR)/Ca+ release channel, are oxidized and subsequently reduced during the process of contraction and relaxation. In this thesis a reagent, o-Phthalaldehyde (OPA), was used to better understand the gating mechanism of the RyR/Ca+ release channel. This reagent has the ability to form an isoindole derivative with the amino acids cysteine and lysine, if they are separated by not more than 3 A .In this study, it was shown that OP A interacts directly with the Ca+ release channel by forming a covalent derivative with a critical thiol and a nearby lysine. High affinity [3H]Ryanodine binding to the RyR\Ca+ release channel is activated by < 130μM OP A, but is inhibited by OPA at concentrations ranging from 200-300 μM OPA. This biphasic behavior indicates that at least two sets of cysteine-lysine pairs regulate Ca+ channel activity. Moreover, the binding of OP A results in increasing the affinity of the receptor for the binding of ryanodine, in a Ca+ independent manner, which may indicate that there are two different sets of RyR\Ca+ release channels present in the SR.

O-Phthalaldehyde Modification of Sarcoplasmic Reticulum Calcium Release