(Q28268338)

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Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. Functional consequences of substitutions of His10, His187 and Arg89

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Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. Functional consequences of substitutions of His10, His187 and Arg89 (English)

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M C Garel

1

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V Lemarchandel

series ordinal

2

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M C Calvin

series ordinal

3

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N Arous

series ordinal

4

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C T Craescu

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5

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M O Prehu

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6

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J Rosa

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7

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R Rosa

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8

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language of work or name

English

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publication date

1 April 1993

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published in

FEBS Journal

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volume

213

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page(s)

493-500

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issue

1

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cites work

Diphosphoglycerate mutase and 2,3-diphosphoglycerate phosphatase activities of red cells: comparative electrophoretic study.

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Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1993.TB17786.X

retrieved

21 January 2018

The identification of glycolate-2-P as a constituent of normal red blood cells

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1993.TB17786.X

retrieved

21 January 2018

Human bisphosphoglycerate mutase expressed in E coli: purification, characterization and structure studies.

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1993.TB17786.X

retrieved

21 January 2018

Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1993.TB17786.X

retrieved

21 January 2018

Identifiers

DOI

10.1111/J.1432-1033.1993.TB17786.X

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PubMed ID

8477721

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ResearchGate publication ID

14721036

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(Q28268338)

Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. Functional consequences of substitutions of His10, His187 and Arg89

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