(Q66953163)

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Argininosuccinase from bovine brain: Isolation and comparison of catalytic, physical, and chemical properties with the enzymes from liver and kidney

scientific article published on 01 May 1979

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1 September 2019

Argininosuccinase from bovine brain: isolation and comparison of catalytic, physical, and chemical properties with the enzymes from liver and kidney (English)

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1 September 2019

Argininosuccinase from bovine brain: Isolation and comparison of catalytic, physical, and chemical properties with the enzymes from liver and kidney (English)

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10.1016/0003-2697(79)90197-0

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11 June 2023

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10.1016/0003-2697(79)90197-0

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11 June 2023

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11 June 2023

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11 June 2023

Kimiko Murofushi

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K Murakami-Murofushi

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1 September 2019

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K. Murakami-Murofushi

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11 June 2023

S. Ratner

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1 May 1979

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1 September 2019

full work available at URL

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11 June 2023

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11 June 2023

Analytical Biochemistry

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1 September 2019

95

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1 September 2019

1

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1 September 2019

139-155

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1 September 2019

Enzymes of arginine metabolism in brain.

1

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11 June 2023

A disease, probably hereditary characterised by severe mental deficiency and a constant gross abnormality of aminoacid metabolism.

2

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11 June 2023

Argininosuccinase activity in brain tissue.

4

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10.1016/0003-2697(79)90197-0

https://api.crossref.org/works/10.1016/0003-2697(79)90197-0

11 June 2023

Argininosuccinase from bovine kidney: Comparison of catalytic, physical, and chemical properties with the enzyme from bovine liver

9

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Fructose diphosphatase from rabbit muscle. II. Amino acid composition and activation by sulfhydryl reagents

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Immunological studies of liver, kidney, and muscle fructose 1,6-diphosphatases

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Purification and properties of arginase of rat kidney

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Rapid microdialysis and hydrogen exchange

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The gel-filtration behaviour of proteins related to their molecular weights over a wide range

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The molecular weight of rabbit muscle aldolase and the properties of the subunits in acid solution

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Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups

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Examination of the dissociation of multichain proteins in guanidine hydrochloride by membrane osmometry

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Tissue sulfhydryl groups

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Combinations of specific color reactions useful in the peptide mapping technique

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DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS

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Identifiers

10.1016/0003-2697(79)90197-0

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:495948%20AND%20SRC:MED&resulttype=core&format=json

1 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:495948%20AND%20SRC:MED&resulttype=core&format=json

1 September 2019

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