Work

Studies on the Subunit Structure of Myosin

Year: 1970

Type: article

Abstract: The low molecular weight protein associated with rabbit skeletal myosin has been estimated by gel filtration studies in 5 m guanidine hydrochloride and was found to constitute 9 ± 2% of the myosin mass. We have found that 40 to 50% of the low molecular weight protein can be removed from myosin without any apparent changes in the adenosine-triphosphatase activity. Attempts to remove a larger fraction of low molecular weight protein resulted in a concomitant loss of enzymatic activity. The molecular weight of the major myosin subunit freed of low molecular weight protein has been redetermined in 5 m guanidine hydrochloride and was found to be 194,000 g per mole. The significance of its presence in assessing the molecular weight of the major subunit at low speed and high speed sedimentation equilibrium has been investigated.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)63416-7

Authors: Joseph Gazith, Sylvia Himmelfarb, William F. Harrington

Institution: Johns Hopkins University

Language: English

Topic: Cardiomyopathy and Myosin Studies

Subfield: Cardiology and Cardiovascular Medicine

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1507842415

FWCI: 23.66

Cites: 32

Cited by: 198

Related to: 10