September 1, 1987Journal of Biological ChemistryOpen Access

Intramolecular cross-linking at the active site of the Ca2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P.

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Population

Ca2+-ATPase of sarcoplasmic reticulum

Design

Preclinical

Authors

DRDavid RossSouth African Medical Research Council DMDavid B. McIntoshUniversity of Cape Town

Discussion

Member takes

Implication

Hypothesis-generating for SERCA conformational states; leaves open relevance to cardiac Ca2+ handling in vivo.

Structured PICO

Population

Ca2+-ATPase of sarcoplasmic reticulum

Intervention

Glutaraldehyde cross-linking in the presence of various nucleotides (ATP, ADP, AMPPCP, trinitrophenyladenosine triphosphate, decavanadate) and phosphorylation states

Outcome

Intramolecular cross-linking at the active site detected by anomalous increase in apparent molecular weight on SDS-PAGEsurrogate

The inability to cross-link the active site of the E2-P intermediate suggests a unique closed active site conformation linked to low affinity, inwardly orientated Ca2+-binding sites.

Cite This Study

Ross et al. (1987) studied this question.

synapsesocial.com/papers/6a7d065bc7e6f6a50737cade https://doi.org/10.1016/s0021-9258(18)45153-8

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Intramolecular cross-linking at the active site of the Ca2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Intramolecular cross-linking at the active site of the Ca2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider