The influence of ethylenediaminetetraacetate on white skeletal muscle myosin

Kasman, Krystyna; Kakol, I

doi:10.1016/0005-2795(77)90295-1

Biochimica et Biophysica Acta (BBA) - Protein Structure

1977

DOI: 10.1016/0005-2795(77)90295-1

|View full text |Cite

The influence of ethylenediaminetetraacetate on white skeletal muscle myosin

Krystyna Kasman

I Kakol

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1978

1981

Publication Types

Select...

Article6

Relationship

Self Cite0

Independent6

Authors

Journals

Cited by 9 publications

(1 citation statement)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Factors that cause dissociation of light chain LC2 may also cause alterations in the swivel region of myosin. Light chain LC2 is more firmly attached to myosin in the presence of Ca2+ (Szent-Gyorgyi, 1975;Kasman & Kadol, 1977). When in association with the heavy chains the binding of Ca2+ is weaker at pH 6.5 as compared with pH 7.4 (Wikman-Coffelt, Muhlrad et al, 1962;Werber, 1978).…”

mentioning

confidence: 99%

Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2

Srivastava

Mühlrád

Wikman‐Coffelt

1981

Biochemical Journal

View full text Add to dashboard Cite

The association of myosin light chains with heavy chains, i.e. the intact oligomeric structure, profoundly affects the Ca(2+)-binding properties of the light chains. The Ca(2+)-binding affinity of the light chains is more than two magnitudes higher in the presence of heavy chains than in its absence. Modification of the reactive SH(2) thiol of myosin results in an alteration in the conformation of heavy chains of the molecule that influences the Ca(2+)-binding properties of light chains and generation of tension. When the SH(2) moiety is blocked with N-ethylmaleimide the influence of the heavy chains on the Ca(2+)-binding properties of light chain LC(2) is lost; under these conditions the Ca(2+)-binding affinity value of SH(2)-N-ethylmaleimide-blocked myosin (3.3x10(4)m(-1)) decreases to near that expressed with the dissociated light chain LC(2) (0.7x10(4)m(-1)). Conversely, the presence of actin, nucleotides or modification of either the reactive lysyl residue or SH(2) thiol does not affect Ca(2+) binding. The native secondary and tertiary structure of myosin seem to be required for Ca(2+) binding; binding does not occur in the presence of 6m-urea with either native myosin or the dissociated light chains. With SH(2)-N-ethylmaleimide-blocked myosin normal Ca(2+)- and (Mg(2+)+actin)-stimulated ATPase activities are expressed; however, there is a loss in K(+)-stimulated ATPase activity and the synthetic actomyosin threads of such myosin express no isometric tension. There are also variances in the binding of Ca(2+) with alterations in pH values. In the absence of Ca(2+)/EGTA buffer the biphasic Ca(2+)-binding affinity of myosin is twice as high at pH7.4 (site one: 1.2x10(6)m(-1) and site two: 0.4x10(6)m(-1)) as compared with values obtained at pH6.5 (site one: 0.64x10(6)m(-1) and site two: 0.2x10(6)m(-1)). The Ca(2+)-binding affinity of light chain LC(2) and S(1), where the (S-1)-(S-2) junction was absent, were not influenced by changes in pH values. Both expressed a low Ca(2+)-binding affinity, approx. 0.7x10(4)m(-1), whereas heavy meromyosin, where both (S-1) and (S-2) myosin subfragments were present, expressed a Ca(2+)-binding affinity value similar to that of native myosin, but was not biphasic. However, it is important to point out than in preparation of S(1) myosin subfragment light chain LC(2) was lost and thus was added back to the purified S(1) fraction. Light chain LC(2) was not, however, added to the heavy meromyosin fraction because it was not lost during preparation of the heavy meromyosin subfragment. In conclusion, it appears that the (S-1)-(S-2) junction is needed for the positioning of light chain LC(2) and thus influences its essential conformation for Ca(2+) binding.

show abstract

mentioning

confidence: 99%

Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2

Srivastava

Mühlrád

Wikman‐Coffelt

1981

Biochemical Journal

View full text Add to dashboard Cite

show abstract

Divalent metal ion binding and subunit interactions in myosins: a critical review

Bagshaw

1980

J Muscle Res Cell Motil

View full text Add to dashboard Cite

The effects of divalent cations on the rotational mobility of myosin, heavy meromyosin and myosin subfragment-1 and on the binding of heavy meromyosin to actin

Highsmith

1978

Biochimica et Biophysica Acta (BBA) - Protein Structure

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

The influence of ethylenediaminetetraacetate on white skeletal muscle myosin

Cited by 9 publications

References 12 publications

Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2

Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2

Divalent metal ion binding and subunit interactions in myosins: a critical review

The effects of divalent cations on the rotational mobility of myosin, heavy meromyosin and myosin subfragment-1 and on the binding of heavy meromyosin to actin

Contact Info

Product

Resources

About