The adenosine triphosphatase activity of the meromyosins

A. Mühlrád; S. Bosko; N. A. Biró

doi:10.1016/0005-2744(67)90199-4

The adenosine triphosphatase activity of the meromyosins

A. Mühlrád^*, S. Bosko, N. A. Biró

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

1. 1.|Mg²⁺ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3. 3.|Acto-HMM does not show Ca²⁺ sensitivity, i.e. its ATPase activity is not inhibited by the removal of Ca²⁺ with ethyleneglycol-bis(aminoethyl)-tetraacetic acid. 4. 4.|The enzymic characteristics of the ATPase-active component of light meromyosin (LMM) preparations are the same as those of heavy meromyosin (HMM). 5. 5.|The ATPase-active component of LMM preparations can be removed from the preparation by ultracentrifugation in the presence of actin in 0.5 M KCl.

Original language	English
Pages (from-to)	138-144
Number of pages	7
Journal	BBA - Enzymology
Volume	132
Issue number	1
DOIs	https://doi.org/10.1016/0005-2744(67)90199-4
State	Published - 11 Jan 1967
Externally published	Yes

Access to Document

10.1016/0005-2744(67)90199-4

Cite this

@article{b498bb96af2745e590af4627679ebacd,

title = "The adenosine triphosphatase activity of the meromyosins",

abstract = "1. 1.|Mg2+ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3. 3.|Acto-HMM does not show Ca2+ sensitivity, i.e. its ATPase activity is not inhibited by the removal of Ca2+ with ethyleneglycol-bis(aminoethyl)-tetraacetic acid. 4. 4.|The enzymic characteristics of the ATPase-active component of light meromyosin (LMM) preparations are the same as those of heavy meromyosin (HMM). 5. 5.|The ATPase-active component of LMM preparations can be removed from the preparation by ultracentrifugation in the presence of actin in 0.5 M KCl.",

author = "A. M{\"u}hlr{\'a}d and S. Bosko and Bir{\'o}, {N. A.}",

year = "1967",

month = jan,

day = "11",

doi = "10.1016/0005-2744(67)90199-4",

language = "אנגלית",

volume = "132",

pages = "138--144",

journal = "BBA - Enzymology",

issn = "0005-2744",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - The adenosine triphosphatase activity of the meromyosins

AU - Mühlrád, A.

AU - Bosko, S.

AU - Biró, N. A.

PY - 1967/1/11

Y1 - 1967/1/11

N2 - 1. 1.|Mg2+ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3. 3.|Acto-HMM does not show Ca2+ sensitivity, i.e. its ATPase activity is not inhibited by the removal of Ca2+ with ethyleneglycol-bis(aminoethyl)-tetraacetic acid. 4. 4.|The enzymic characteristics of the ATPase-active component of light meromyosin (LMM) preparations are the same as those of heavy meromyosin (HMM). 5. 5.|The ATPase-active component of LMM preparations can be removed from the preparation by ultracentrifugation in the presence of actin in 0.5 M KCl.

AB - 1. 1.|Mg2+ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3. 3.|Acto-HMM does not show Ca2+ sensitivity, i.e. its ATPase activity is not inhibited by the removal of Ca2+ with ethyleneglycol-bis(aminoethyl)-tetraacetic acid. 4. 4.|The enzymic characteristics of the ATPase-active component of light meromyosin (LMM) preparations are the same as those of heavy meromyosin (HMM). 5. 5.|The ATPase-active component of LMM preparations can be removed from the preparation by ultracentrifugation in the presence of actin in 0.5 M KCl.

UR - http://www.scopus.com/inward/record.url?scp=0014199609&partnerID=8YFLogxK

U2 - 10.1016/0005-2744(67)90199-4

DO - 10.1016/0005-2744(67)90199-4

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 4226532

AN - SCOPUS:0014199609

SN - 0005-2744

VL - 132

SP - 138

EP - 144

JO - BBA - Enzymology

JF - BBA - Enzymology

IS - 1

ER -

The adenosine triphosphatase activity of the meromyosins

Abstract

Access to Document

Other files and links

Fingerprint

Cite this