Polymerization of proteins with glutaraldehyde. Soluble molecular-weight markers (Q42558388)

2 November 2017

Polymerization of proteins with glutaraldehyde. Soluble molecular-weight markers (English)

1 reference

2 November 2017

J W Payne

1

1 reference

PMCID

1165906

2 November 2017

language of work or name

English

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publication date

1 December 1973

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2 November 2017

7

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inferred from page(s)

published in

Biochemical Journal

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2 November 2017

135

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2 November 2017

867-873

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2 November 2017

4

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INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A

2 November 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Some aspects of fixation with glutaraldehyde. A biochemical and histochemical comparison of the effects of formaldehyde and glutaraldehyde fixation on various enzymes and glycogen, with a note on penetration of glutaraldehyde into liver

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

The effect of cross-links on the mobility of proteins in dodecyl sulphate–polyacrylamide gels

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

A comparison of the crosslinking abilities of glutaraldehyde, formaldehyde and alpha-hydroxyadipaldehyde with bovine serum albumin and casein.

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugates for the detection of antigens and antibodies.

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Fixatives and fixation: a review

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents.

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity.

28 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1165906

Observations on Molecular Weight Determinations on Polyacrylamide Gel

16 August 2018

1 reference

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Properties and enzymatic activities of papain insolubilized with glutaraldehyde

16 August 2018

1 reference

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Automated determination of bacterial asparaginase and glutaminase

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Proteins coupled to polyacrylamide beads using glutaraldehyde

1 reference

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Glutaraldehyde as a protein cross-linking reagent

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Preparation of enzymically active, water-insoluble derivatives of trypsin

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Reaction of proteins with glutaraldehyde

1 reference

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Intermolecular cross-linking of monomeric proteins and cross-linking of oligomeric proteins as a probe of quaternary structure. Application to leucine aminopeptidase (bovine lens)

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Bifunctional Reagents for the Crosslinking of Proteins

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Preparation of water-insoluble, enzymatically active derivatives of subtilisin type Novo by cross-linking with glutaraldehyde

1 reference

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Preparation and properties of crosslinked water-insoluble catalase

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Modification of papain by treatment with glutaraldehyde under reducing and non-reducing conditions

1 reference

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The reactions between glutaraldehyde and various proteins. An investigation of their kinetics

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Glutaraldehyde, cyanuric choloride and tetraazotiexe O-dianisidine as coupling reagents in the passive hemagglutination test

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Identifiers

DOI

10.1042/BJ1350867

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2 November 2017

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2 November 2017

1 reference

PMCID

1165906