(Q42916180)

11 November 2017

Evidence for an active dimer of Escherichia coli beta-galactosidase (English)

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11 November 2017

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Kaneshiro CM

1

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11 November 2017

Enns CA

2

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11 November 2017

Hahn MG

3

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11 November 2017

Peterson JS

4

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11 November 2017

Reithel FJ

5

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11 November 2017

language of work or name

English

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publication date

1 November 1975

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11 November 2017

2

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based on heuristic

inferred from page(s)

published in

Biochemical Journal

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11 November 2017

151

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11 November 2017

2

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11 November 2017

433-434

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Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads

11 November 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1172374

Studies on protein multimers. The association–dissociation behaviour of β-galactosidase in glycerol

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1172374

Studies on protein multimers. V. Further characterization of beta-galactosidase self-association behavior with observations on apparent specific volume

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1172374

A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1172374

Purification and characterization of the multiple forms of β-galactosidase of Escherichia coli

16 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1172374

16 August 2018

Identifiers

DOI

10.1042/BJ1510433

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11 November 2017

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11 November 2017

PubMed publication ID

766750

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