Gel Isoelectric Focusing of Selected Bovine Immunoglobulins

Josephson, R.V.; Mikolajick, E.M.; Sinha, D.P.

doi:10.3168/jds.s0022-0302(72)85705-9

Cited by 16 publications

(11 citation statements)

References 7 publications

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“…In contrast to BSA, the distribution of IgG shifted only slightly toward the anode after 5.0 min, as shown in Figure c,d. This is primarily because IgG has a different isoelectric point than BSA: 7.3 ± 1.0 and 4.9 ± 0.1, , respectively (recall that the separation is carried out at pH 7.4). Additionally, IgG is a larger molecule (∼150 kDa) than BSA (∼66.5 kDa), which also leads to a lower mobility.…”

Section: Resultsmentioning

confidence: 99%

Low-Voltage Origami-Paper-Based Electrophoretic Device for Rapid Protein Separation

Luo

Crooks

2014

Anal. Chem.

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We present an origami paper-based electrophoretic device (oPAD-Ep) that achieves rapid (∼5 min) separation of fluorescent molecules and proteins. Due to the innovative design, the required driving voltage is just ∼10 V, which is more than 10 times lower than that used for conventional electrophoresis. The oPAD-Ep uses multiple, thin (180 μm/layer) folded paper layers as the supporting medium for electrophoresis. This approach significantly shortens the distance between the anode and cathode, and this, in turn, accounts for the high electric field (>1 kV/m) that can be achieved even with a low applied voltage. The multilayer design of the oPAD-Ep enables convenient sample introduction by use of a slip layer as well as easy product analysis and reclamation after electrophoresis by unfolding the origami paper and cutting out desired layers. We demonstrate the use of oPAD-Ep for simple separation of proteins in bovine serum, which illustrates its potential applications for point-of-care diagnostic testing.

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Section: Resultsmentioning

confidence: 99%

Low-Voltage Origami-Paper-Based Electrophoretic Device for Rapid Protein Separation

Luo

Crooks

2014

Anal. Chem.

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“…2) formed an arc which extended entirely towards the anode; a similar pattern was reported by Berne, Dray & Knight (1970) for rabbit a 2 macroglobulin allotypes. It has been shown that cattle IgM, on the other hand, form a precipitation arc close to the origin and extended on both anodic and cathodic sides of the well (Butler, 1969;Josephson, Mikolajick & Sinha, 1972).…”

Section: Discussionmentioning

confidence: 98%

Immunogenetics of a macroglobulin allotype in cattle

Iannelli

Masina

1978

Genet. Res.

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“…The author suggests that heated BSA precipitates with CN at pH 4.7 and does not interact with CN during heating. The IgG and LFR were present in the filtrate but not in the precipitate (Table 3), and this might be because the isoelectric point of these proteins are higher than 4.6, which is the isoelectric point of CN (Josephson et al, 1972;Liang et al, 2011).…”

Section: Quantification Of Cn Cnpp and Sp (%) In Kjeldahl Ncn Filtrate And Ncn Precipitatementioning

confidence: 99%

Measurement of casein in milk by Kjeldahl and sodium dodecyl sulfate–polyacrylamide gel electrophoresis

Marzo

Pranata

Barbano

2021

Journal of Dairy Science

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Our objectives were to determine if milk casein as a percentage of true protein (CN%TP) estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is equivalent to CN%TP estimated by Kjeldahl, and to determine the proportion of casein (CN), casein proteolysis products (CNPP), and serum protein (SP) from milk true protein (TP) that goes into the Kjeldahl noncasein nitrogen (NCN) filtrate and the proportion that stays in the NCN precipitate using SDS-PAGE. Raw milk samples were collected from 16 mid-lactation Holstein cows twice a week for 2 wk.

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Gel Isoelectric Focusing of Selected Bovine Immunoglobulins

Cited by 16 publications

References 7 publications

Low-Voltage Origami-Paper-Based Electrophoretic Device for Rapid Protein Separation

Low-Voltage Origami-Paper-Based Electrophoretic Device for Rapid Protein Separation

Immunogenetics of a macroglobulin allotype in cattle

Measurement of casein in milk by Kjeldahl and sodium dodecyl sulfate–polyacrylamide gel electrophoresis

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