Limited autolysis reduces the Ca2 requirement of a smooth muscle Ca2 -activated protease (Q72936356)

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30 October 2019

title

Limited autolysis reduces the Ca2 requirement of a smooth muscle Ca2 -activated protease (English)

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30 October 2019

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16 September 2023

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16 September 2023

author name string

D. R. Hathaway

1

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16 September 2023

D. K. Werth

2

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16 September 2023

J. R. Haeberle

3

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16 September 2023

language of work or name

English

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publication date

1 August 1982

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30 October 2019

10 August 1982

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=6284756

full work available at URL

16 September 2023

http://intl.jbc.org/cgi/content/abstract/257/15/9072

online access status

open access

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https://api.elsevier.com/content/article/PII:S0021925818342443?httpAccept=text/xml

16 September 2023

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https://api.elsevier.com/content/article/PII:S0021925818342443?httpAccept=text/plain

16 September 2023

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https://api.crossref.org/works/10.1016/S0021-9258(18)34244-3

Journal of Biological Chemistry

16 September 2023

published in

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30 October 2019

volume

257

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30 October 2019

issue

15

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30 October 2019

page(s)

9072-9077

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Activation of skeletal muscle phosphorylase kinase by Ca2 . II. Identification of the kinase activating factor as a proteolytic enzyme

30 October 2019

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Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization

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Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle

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Properties of a calcium-activated protease in squid axoplasm which selectively degrades neurofilament proteins

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Purification and some characteristics of a Ca2 -activated proteolytic enzyme from beef cardiac muscle

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Purification and characterization of a calcium dependent sulfhydryl protease from human platelets

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Canine cardiac calcium-dependent proteases: Resolution of two forms with different requirements for calcium

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Limited Autolysis of Ca2 -Activated Neutral Protease (CANP) Changes Its Sensitivity to Ca2 Ions

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A new method for the preparation of a calcium activated neutral protease highly sensitive to calcium ions

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A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the protease

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Phosphorylation of low molecular weight proteins in purified preparations of rat heart sarcolemma and sarcoplasmic reticulum

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Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity

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Purification and properties of myosin light-chain kinase from fast skeletal muscle

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Separation of Low Molecular Weight Components of Pig Cardiac Myosin and Myosin Subfragment-1, and Ca2 Binding to One of the Components (g2)1

16 September 2023

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Re-examination of the apparent binding constant of ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid with calcium around neutral pH

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A Ca2 -activated protease possibly involved in myofibrillar protein turnover. Subcellular localization of the protease in porcine skeletal muscle

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16 September 2023

Identifiers

1 reference