June 1, 1976Canadian Journal of Biochemistry

The isolation and characterization of the tropomyosin binding component (TN-T) of bovine cardiac troponin

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Population

Bovine cardiac muscle

Design

Preclinical

Authors

LBLeslie D. BurtnickUniversity of British Columbia WMWilliam D. McCubbinUniversity of Alberta CKC.M. KayNew Mexico State University

Discussion

Member takes

Implication

Characterizes conserved troponin interactions in bovine cardiac muscle; leaves open translation to human cardiac regulation in vivo.

Structured PICO

Population

Bovine cardiac muscle

Intervention

Purification and characterization of the tropomyosin binding component (TN-T) of troponin using ion exchange chromatographies in the presence of urea

Outcome

Physical and chemical properties of TN-T (molecular weight, alpha-helical content) and its interactions with TN-C and tropomyosinsurrogate

The isolation and characterization of bovine cardiac TN-T demonstrate its physical properties and interactions with TN-C and tropomyosin, indicating a regulatory mechanism similar to skeletal muscle.

Cite This Study

Burtnick et al. (1976) studied this question.

synapsesocial.com/papers/6a7d4da600c5c9efbcaa1806 https://doi.org/10.1139/o76-080

View Full Paper

Ask AI

Bookmark

The isolation and characterization of the tropomyosin binding component (TN-T) of bovine cardiac troponin

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The isolation and characterization of the tropomyosin binding component (TN-T) of bovine cardiac troponin

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider