Immune serum to protein molecular weight standards for calibrating Western blots

Carlone, George M.; Plikaytis, Bonnie B.; Arko, R J

doi:10.1016/0003-2697(86)90229-0

Analytical Biochemistry

1986

DOI: 10.1016/0003-2697(86)90229-0

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Immune serum to protein molecular weight standards for calibrating Western blots

George M. Carlone

Bonnie B. Plikaytis

R J Arko

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1987

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Cited by 9 publications

(1 citation statement)

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“…Rabbit immune serum was diluted 1:500, and goat anti-rabbit immunoglobulin-horseradish peroxidase conjugate (Sigma) was diluted 1:1,000 in TSEA-Tw. Standards were visualized by anti-standard rabbit sera as described by Carlone et al (2). Antisera prepared with formalinized whole-cell vaccines of the type strains of 23 Legionella species (12) were from the Immunology Laboratory of the Centers for Disease Control.…”

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confidence: 99%

Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen

et al. 1988

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A genuswide protein antigen extracted from LegioneUa pneumophila serogroup 1 (strain Philadelphia 1) cells was enriched by differential pelleting and ammonium sulfate precipitation and subsequently purified with a combination of high-performance size-exclusion and ion-exchange chromatography. The protein has an apparent molecular weight of 650,000 before and 63,000 after urea (5 M) treatment, as determined by size-exclusion chromatography. These proteins resolved to a single band of 60,000 after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The urea-treated protein had an isoelectric point of 5.8. This purified 60-kilodalton protein reacted with a convalescent-phase serum sample from a patient with legionellosis and rabbit immune sera prepared against each of 23 Legionella species. The 60-kilodalton protein may be useful in developing diagnostic tests for legionellosis.

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confidence: 99%

Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen

et al. 1988

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Visualization of molecular weight standards after electroblotting: Detection by means of corresponding antibodies

Bjerrum

Hinnerfeldt

1987

Electrophoresis

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The techniques available for detection of molecular weight standards after blotting are surveyed and evaluated. An identical immunodetection procedure for the antigens as well as for the molecular weight markers was evaluated by immunizing rabbits with the whole protein mixture of some commercially available calibration kits for sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Antibodies against both high and low molecular weight proteins were successfully raised albeit one rabbit failed to generate antibodies against ovalbumin. For immunodetection of rabbit myosin it was necessary to supplement the immunogen with bovine myosin. Best results were obtained by using more than one animal immunized with kits of different origin. Using alkaline phosphatase conjugated secondary antibodies, as little as 0.6 and 1.2 1. 18 of the total low and high molecular weight mixture, respectively, are necessary for the immunoenzymatic detection of all bands. In fused rocket immunoelectrophoresis such antibodies are also useful for determination of the elution position of the molecular weight markers in gel filtration experiments.

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Gamma globulin-derived standards for the determination of molecular weights, transfer, and immunodetection efficiencies in protein blotting procedures

Davies

Gilbo

Marley

et al. 1989

Analytical Biochemistry

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Immune serum to protein molecular weight standards for calibrating Western blots

Cited by 9 publications

References 16 publications

Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen

Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen

Visualization of molecular weight standards after electroblotting: Detection by means of corresponding antibodies

Gamma globulin-derived standards for the determination of molecular weights, transfer, and immunodetection efficiencies in protein blotting procedures

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