(Q47182617)

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Proteolysis of the protein inhibitor of calcium-dependent proteases produces lower molecular weight fragments that retain inhibitory activity

scientific article published on April 1, 1988

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Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/3355165

Proteolysis of the protein inhibitor of calcium-dependent proteases produces lower molecular weight fragments that retain inhibitory activity (English)

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10.1016/0003-9861(88)90181-6

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30 December 2022

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30 December 2022

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10.1016/0003-9861(88)90181-6

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30 December 2022

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G. N. DeMartino

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A3355165

30 December 2022

R. Wachendorfer

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A3355165

30 December 2022

M. J. McGuire

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30 December 2022

D. E. Croall

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30 December 2022

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1 April 1988

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11 January 2018

http://europepmc.org/abstract/MED/3355165

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https://api.elsevier.com/content/article/PII:0003986188901816?httpAccept=text/xml

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10.1016/0003-9861(88)90181-6

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30 December 2022

https://api.elsevier.com/content/article/PII:0003986188901816?httpAccept=text/plain

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10.1016/0003-9861(88)90181-6

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Archives of Biochemistry and Biophysics

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PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/3355165

262

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11 January 2018

http://europepmc.org/abstract/MED/3355165

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11 January 2018

http://europepmc.org/abstract/MED/3355165

189-198

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Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/3355165

Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules.

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The appearance of a 34,000-dalton inhibitor of calpain (Ca2+-dependent cysteine proteinase) in rat liver after the administration of phenylhydrazine

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Purification of a high-molecular-weight inhibitor of the calcium-activated proteinase

6

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Purification and characterization of a protein inhibitor of calcium-dependent proteases from rat liver

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The protein inhibitor of calcium-dependent proteases: Purification from bovine heart and possible mechanisms of regulation

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Comparison of two calcium-dependent proteinases from bovine heart

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Fluorometric assay of secondary amino acids.

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Fluorescamine: A Reagent for Assay of Amino Acids, Peptides, Proteins, and Primary Amines in the Picomole Range

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Purification and characterization of a high molecular weight proteinase (macropain) from human erythrocytes

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Evidence for non-competitive inhibition between two calcium-dependent activated neutral proteinases and their specific inhibitor

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The occurrence of an inhibitor of Ca2+-dependent neutral protease in rat liver

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Purification and some properties of human erythrocyte calpastatin

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Purification and characterization of 210,000-dalton inhibitor of calcium-activated neutral protease from rabbit skeletal muscle and its relation to 50,000-dalton inhibitor

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Role of Ca2+ and Ca2+-activated protease in myoblast fusion

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Molecular diversity of calpastatin in mammalian organs

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Proteolysis of the calcium-dependent protease inhibitor by myocardial calcium-dependent protease

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Evidence for the repetitive domain structure of pig calpastatin as demonstrated by cloning of complementary DNA.

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Repetitive region of calpastatin is a functional unit of the proteinase inhibitor

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A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity

26

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10.1016/0003-9861(88)90181-6

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Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/3355165

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PubMed publication ID

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Europe PubMed Central

PubMed publication ID

11 January 2018

http://europepmc.org/abstract/MED/3355165

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