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Journal articles on the topic 'Gel electrophoresis'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 July 2024

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1

Ohshima, Hiroyuki. "Transient Gel Electrophoresis of a Spherical Colloidal Particle." Gels 9, no. 5 (April 23, 2023): 356. http://dx.doi.org/10.3390/gels9050356.

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The general theory is developed for the time-dependent transient electrophoresis of a weakly charged spherical colloidal particle with an electrical double layer of arbitrary thickness in an uncharged or charged polymer gel medium. The Laplace transform of the transient electrophoretic mobility of the particle with respect to time is derived by considering the long-range hydrodynamic interaction between the particle and the polymer gel medium on the basis of the Brinkman–Debye–Bueche model. According to the obtained Laplace transform of the particle’s transient electrophoretic mobility, the transient gel electrophoretic mobility approaches the steady gel electrophoretic mobility as time approaches infinity. The present theory of the transient gel electrophoresis also covers the transient free-solution electrophoresis as its limiting case. It is shown that the relaxation time for the transient gel electrophoretic mobility to reach its steady value is shorter than that of the transient free-solution electrophoretic mobility and becomes shorter as the Brinkman screening length decreases. Some limiting or approximate expressions are derived for the Laplace transform of the transient gel electrophoretic mobility.

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2

Tan, Timothy Ter Ming, Zong Ying Tan, Wei Liang Tan, and Peng Foo Peter Lee. "Gel electrophoresis." Biochemistry and Molecular Biology Education 35, no. 5 (2007): 342–49. http://dx.doi.org/10.1002/bmb.83.

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3

Yamanaka, Masamichi. "Supramolecular gel electrophoresis." Polymer Journal 50, no. 8 (March 15, 2018): 627–35. http://dx.doi.org/10.1038/s41428-018-0033-y.

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4

ünlü, M. "Difference gel electrophoresis." Biochemical Society Transactions 27, no. 4 (August 1, 1999): 547–49. http://dx.doi.org/10.1042/bst0270547.

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5

Raymond, Samuel. "ACRYLAMIDE GEL ELECTROPHORESIS." Annals of the New York Academy of Sciences 121, no. 2 (December 16, 2006): 350–65. http://dx.doi.org/10.1111/j.1749-6632.1964.tb14208.x.

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6

Maddox, John. "Understanding gel electrophoresis." Nature 345, no. 6274 (May 1990): 381. http://dx.doi.org/10.1038/345381a0.

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7

Studier, F. "Slab-gel electrophoresis." Trends in Biochemical Sciences 25, no. 12 (December 1, 2000): 588–90. http://dx.doi.org/10.1016/s0968-0004(00)01679-0.

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8

Longbottom, David. "Gel electrophoresis: Proteins." Trends in Genetics 10, no. 3 (March 1994): 107. http://dx.doi.org/10.1016/0168-9525(94)90235-6.

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9

Merrick, B. Alex. "Gel electrophoresis: Proteins." Trends in Cell Biology 4, no. 2 (February 1994): 67–68. http://dx.doi.org/10.1016/0962-8924(94)90016-7.

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10

Righetti, Pier Giorgio. "Gel electrophoresis: Proteins." Journal of Chromatography A 662, no. 1 (February 1994): 200–201. http://dx.doi.org/10.1016/0021-9673(94)85312-6.

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11

Green, Michael R., and Joseph Sambrook. "Agarose Gel Electrophoresis." Cold Spring Harbor Protocols 2019, no. 1 (January 2019): pdb.prot100404. http://dx.doi.org/10.1101/pdb.prot100404.

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12

Green, Michael R., and Joseph Sambrook. "Polyacrylamide Gel Electrophoresis." Cold Spring Harbor Protocols 2020, no. 12 (December 2020): pdb.prot100412. http://dx.doi.org/10.1101/pdb.prot100412.

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13

Sambrook, Joseph, and David W. Russell. "Agarose Gel Electrophoresis." Cold Spring Harbor Protocols 2006, no. 1 (June 2006): pdb.prot4020. http://dx.doi.org/10.1101/pdb.prot4020.

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14

Görg, Angelika. "Gel electrophoresis: Proteins." FEBS Letters 344, no. 2-3 (May 16, 1994): 266. http://dx.doi.org/10.1016/0014-5793(94)00174-x.

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15

Minden, Jonathan S., Susan R. Dowd, Helmut E. Meyer, and Kai Stühler. "Difference gel electrophoresis." ELECTROPHORESIS 30, S1 (June 2009): S156—S161. http://dx.doi.org/10.1002/elps.200900098.

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16

Armstrong, Jennifer A., and Joseph R. Schulz. "Agarose Gel Electrophoresis." Current Protocols Essential Laboratory Techniques 00, no. 1 (January 2008): 7.2.1–7.2.20. http://dx.doi.org/10.1002/9780470089941.et0702s00.

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17

Dolník, Vladislav. "Capillary gel electrophoresis." Journal of Microcolumn Separations 6, no. 4 (July 1994): 315–30. http://dx.doi.org/10.1002/mcs.1220060402.

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18

Samelson, L. E. "Diagonal Gel Electrophoresis." Current Protocols in Immunology 00, no. 1 (December 1991): 8.6.1–8.6.4. http://dx.doi.org/10.1002/0471142735.im0806s02.

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19

Timms, John F., and Rainer Cramer. "Difference gel electrophoresis." PROTEOMICS 8, no. 23-24 (December 2008): 4886–97. http://dx.doi.org/10.1002/pmic.200800298.

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20

Kawaguchi, Yoshimasa, and Yu Mikame. "Polyacrylamide Gel Electrophoresis." Drug Delivery System 38, no. 2 (March 25, 2023): 171–76. http://dx.doi.org/10.2745/dds.38.171.

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21

Barberis, Lucila Isabel, Alberto Jorge Eraso, Maria Cristina Pàjaro, and Inès Albesa. "Molecular weight determination and partial characterization of Klebsiella pneumoniae hemolysins." Canadian Journal of Microbiology 32, no. 11 (November 1, 1986): 884–88. http://dx.doi.org/10.1139/m86-161.

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Two thiol-activated Klebsiella pneumoniae hemolysins were purified from growth media by means of salt precipitation, gel filtration, ion-exchange chromatography, and polyacrylamide gel electrophoresis. The hemolysins peaks coincided with the protein and glycoprotein peaks as determined by chromatography and electrophoresis, The molecular weights, estimated by gel filtration, were 8400 and 19 000; by sodium dodecyl sulphate–polyacrylamide gel electrophoresis, the values were calculated as 15 500 and 27 000. The electrophoretic bands were best detected by the periodic acid–Schiff method. Reduction of the disulfide linkages did not cause the originally larger molecule to break into 8400 and 19 000 hemolysins. However, trypsin treatment cleaved the 19 000 hemolysin into an active moiety, with an electrophoretic migration similar to the 8400 hemolysin. A naturally occurring proteolytic activity was investigated using pepstatin and antipain. When the trypsin inhibitor was added to the system, the hemolytic activity was detected only in the 19 000 hemolysin and the smaller hemolysin was absent.

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22

Hill, Reghan J. "Hydrogel charge regulation and electrolyte ion-concentration perturbations in nanoparticle gel electrophoresis." Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences 471, no. 2184 (December 2015): 20150523. http://dx.doi.org/10.1098/rspa.2015.0523.

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Gel electrophoresis of spherical nanoparticles (NPs) is studied using an electrokinetic model that couples the ion conservation equations to the Poisson and fluid momentum equations, thus including the so-called polarization and relaxation processes. This model is therefore the charged gel electrophoresis analogue of the well-known O’Brien and White solution of the standard electrokinetic model for free-solution electrophoresis. Results are provided for the small NPs (size around 10 nm) to which gel electrophoresis is relevant, because particles must be small enough to permeate the gel: these include the particle drag coefficient (or Brownian diffusivity), which is subject to hydrodynamic screening and electroviscous effects, and the electrophoretic mobility, which is subject to nonlinear electrostatic and charge polarization influences. Also addressed are the influences of charge-regulating gels and the accompanying particle-induced immobile charge-density perturbations. Ion-concentration perturbations attenuate the electrophoretic mobility and enhance the drag coefficient according to the particle charge and the mobility of the most abundant counterion. However, dynamic regulation of the hydrogel charge—termed the secondary immobile charge-density perturbation—has a negligible influence on the particle mobility, and may therefore be neglected for most practical purposes.

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23

Holland, Lisa A., and Laura D. Casto-Boggess. "Gels in Microscale Electrophoresis." Annual Review of Analytical Chemistry 16, no. 1 (June 14, 2023): 161–79. http://dx.doi.org/10.1146/annurev-anchem-091522-080207.

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Gel matrices are fundamental to electrophoresis analyses of biopolymers in microscale channels. Both capillary gel and microchannel gel electrophoresis systems have produced fundamental advances in the scientific community. These analytical techniques remain as foundational tools in bioanalytical chemistry and are indispensable in the field of biotherapeutics. This review summarizes the current state of gels in microscale channels and provides a brief description of electrophoretic transport in gels. In addition to the discussion of traditional polymers, several nontraditional gels are introduced. Advances in gel matrices highlighted include selective polymers modified to contain added functionality as well as thermally responsive gels formed through self-assembly. This review discusses cutting-edge applications to challenging areas of discovery in DNA, RNA, protein, and glycan analyses. Finally, emerging techniques that result in multifunctional assays for real-time biochemical processing in capillary and three-dimensional channels are identified.

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24

Esser, K. A., M. O. Boluyt, and T. P. White. "Separation of cardiac myosin heavy chains by gradient SDS-PAGE." American Journal of Physiology-Heart and Circulatory Physiology 255, no. 3 (September 1, 1988): H659—H663. http://dx.doi.org/10.1152/ajpheart.1988.255.3.h659.

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Separation of alpha- and beta-myosin heavy chains (MHCs) in cardiac ventricles of rats by gradient sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was accomplished and compared with the separation of myosin isozymes obtained with pyrophosphate gels. Whole muscle homogenates were electrophoresed on a 4–9% linear gradient SDS polyacrylamide gel for 3–4 h. MHC bands were identified by the migration distance relative to a MHC standard and immunoblot results with a monoclonal antibody to MHC. The MHC bands were further identified as alpha and beta based on the electrophoretic mobility of ventricular homogenates from hypothyroid and hyperthyroid rats and ventricular and slow soleus skeletal muscle homogenates from control rats. The beta-MHC migrated faster than alpha-MHC, and laser densitometry revealed separate peaks when both MHCs were present. With homogenates containing MHC ranging from 0 to 100% alpha, the separation of MHCs with gradient SDS-PAGE correlated highly (r = 0.97) with separation of myosin isozymes by pyrophosphate gel electrophoresis. The SDS-PAGE technique reported herein is a quick, valid, and direct method for the identification and quantification of ventricular MHCs.

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25

Cutillas, C., B. Rodriguez, P. German, and D. Guevara. "Isoenzymatic pattern of glucose 6-phosphate dehydrogenase from Ascaris suum." Journal of Helminthology 67, no. 3 (September 1993): 226–32. http://dx.doi.org/10.1017/s0022149x0001316x.

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AbstractThe isoenzymatic pattern of glucose 6-phosphate dehydrogenase (abbreviation G6PD) from Ascaris suum has been studied by vertical polyacrylamide gel (PAGE) and horizontal starch gel electrophoresis. After polyacrylamide gel electrophoresis, two stained zones could be identified. One corresponded to tetrazolium oxidase activity; since this zone was stained even in the absence of glucose 6-phosphate (G6P), non-specific staining could be detected. In the other zone of activity, seven regularly-spaced bands were identified by staining in the presence of G6P and NADP as substrates. By using starch gel electrophoresis, different electrophoretic patterns for G6PD have been observed in the muscular sac, intestine and reproductive system from A. suum. The existence of three different alleles of G6PD in the same individual suggests the existence of at least two genes for this enzyme.

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26

Sajjadi, Sayyed Hashem, Hossein Ahmadzadeh, and Elaheh K. Goharshadi. "Enhanced electrophoretic separation of proteins by tethered SiO2 nanoparticles in an SDS-polyacrylamide gel network." Analyst 145, no. 2 (2020): 415–23. http://dx.doi.org/10.1039/c9an01759c.

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Tethered nanoparticles (NPs) are able to improve the separation efficiency of proteins in SDS-polyacrylamide gel electrophoresis (SDS-PAGE) due to their capability of enhancing heat dissipation during electrophoresis and restriction of electrophoretic movement of NPs.

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27

Konovalova, Olga Yu, Nataliia O. Nikitina, Valentyna Yu Nesterenko, Valeriia S. Savchenko, and Yelyzaveta G. Kobzar. "Gel-Electrophoretic Separation of a Number of Synthetic Food Dyes with Following Determination by Spectrophotometric and Visual Method: Simply and Economically." Methods and Objects of Chemical Analysis 18, no. 3 (2023): 126–35. http://dx.doi.org/10.17721/moca.2023.126-135.

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An aim of investigation was separation of synthetic food dyes E 102, E 110, E 122, E 124, E 129, E 132 and E 133 by method of planar gel-electrophoresis with following detection and determination of analytes directly on gel plate. Agar-agar gel or polyacrylamide gel was used as carrier. The influence of electrophoretic buffer pH, amperage, voltage as well as time of electrophoresis on dyes separation in agar-agar gel was investigated. Changing of dyes mobility with pH changing was explained by analysis of their ionization constants. The results of dyes electrophoretic separation were evaluated directly on gel plate by spectrophotometric and visual methods. The metrological characteristics of dyes spectrophotometric quantification and visual semiquantification after analytes separation were evaluated. The metrological characteristics of visual detection and semi-quantification of dyes were evaluated on the basis of statistical approach and investigation of analyte detection probability distribution in the range of reaction unreliability. The suggested technique of electrophoretic separation and following spectrophotometric or visual determination of dyes was successfully checked in analysis of pharmaceuticals.

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28

Wheeler, Rachel D., Micsha V. Costa, Asante Crichlow, Fenella Willis, Yasmin Reyal, Sarah E. Linstead, and Joanne E. Morris. "Case report: Interference from isatuximab on serum protein electrophoresis prevented demonstration of complete remission in a myeloma patient." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 59, no. 2 (December 23, 2021): 144–48. http://dx.doi.org/10.1177/00045632211062080.

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Multiple myeloma is a haematological cancer caused by malignant plasma cells in the bone marrow that can result in organ dysfunction and death. Recent novel treatments have contributed to improved survival rates, including monoclonal antibody therapies that target the CD38 protein on the surface of plasma cells. Anti-CD38 therapies are IgG kappa monoclonal antibodies that are given in doses high enough for the drug to be visible on serum protein electrophoresis as a small paraprotein. We present a case where isatuximab, the most recent anti-CD38 monoclonal antibody to be approved for treatment of myeloma, obscured the patient’s paraprotein on gel immunofixation, so that complete remission could not be demonstrated. This was resolved using the isatuximab Hydrashift assay. The interference on gel immunofixation was unexpected because isatuximab migrated in a position distinct from the patient’s paraprotein on capillary zone electrophoresis. We demonstrate the surprising finding that isatuximab migrates in a different position on gel electrophoresis compared to capillary zone electrophoresis. It is vital that laboratories are aware of the possible interference on electrophoresis from anti-CD38 monoclonal antibody therapies, and are able to recognise these drugs on protein electrophoresis. The difference in isatuximab’s electrophoretic mobility on capillary and gel protein electrophoresis makes this particularly challenging. Laboratories should have a strategy for alternative analyses in the event that the drugs interfere with assessment of the patient’s paraprotein.

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29

Proverbio, Daniela, Roberta Perego, Luciana Baggiani, Giuliano Ravasio, Daniela Giambellini, and Eva Spada. "Serum Protein Gel Agarose Electrophoresis in Captive Tigers." Animals 10, no. 4 (April 20, 2020): 716. http://dx.doi.org/10.3390/ani10040716.

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Given the endangered status of tigers (Panthera tigris), the health of each individual is important and any data on blood chemistry values can provide valuable information alongside the assessment of physical condition. The nature of tigers in the wild makes it is extremely difficult to obtain biological samples from free-living subjects, therefore the values obtained from captive tigers provide very useful data. Serum protein electrophoresis is a useful tool in the diagnosis and monitoring of a number of diseases. In this study, we evaluated agarose gel serum protein electrophoresis on samples from 11 healthy captive tigers. Serum electrophoresis on all 11 tiger samples successfully separated proteins into albumin, α1, α2, β1, β2 and γ globulin fractions as in other mammals. Electrophoretic patterns were comparable in all tigers. Mean± standard deviation or median and range values obtained for each protein fraction in healthy tigers were, respectively: 3.6 ± 0.2, 0.21 (0.2–0.23), 1.2 ± 0.2, 10.7 ± 0.2, 0.4 (0.3–0.6), 1.2 (1–1.8) gr/dL. The results of this preliminary study provide the first data on serum electrophoretic patterns in tigers and may be a useful diagnostic tool in the health assessment of this endangered species.

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30

Koutny, Lance B., and Edward S. Yeung. "Automated Image Analysis for Distortion Compensation in Sequencing Gel Electrophoresis." Applied Spectroscopy 46, no. 1 (January 1992): 136–41. http://dx.doi.org/10.1366/0003702924444461.

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A computerized method is described for correcting systematic distortion of images from slab gel electrophoresis. Such distortions can lead to misinterpretation of the information contained in the gel. The method is useful for data analysis in one-dimension slab gel electrophoresis where the information is manifested in rectangular shaped bands, such as conventional restriction digest or sequencing gels, and the distortions can be adequately described by continuous low-order polynomial functions. The purpose is to eliminate human skill and judgement from the process and to minimize human interaction, which would be useful in any future attempts to automate the analysis of electrophoretic gels.

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31

Jamasbi, Roudabeh J., Stephen J. Kennel, Larry C. Waters, Linda J. Foote, and J. Michael Ramsey. "Genetic Analysis ofPseudomonas aeruginosaby Enterobacterial Repetitive Intergenic Consensus Polymerase Chain Reaction (PCR) and Arbitrarily Primed PCR: Gel Analysis Compared with Microchip Gel Electrophoresis." Infection Control & Hospital Epidemiology 25, no. 1 (January 2004): 65–71. http://dx.doi.org/10.1086/502295.

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AbstractObjectives:To assess the applicability of a newly emerging microchip gel electrophoresis for rapid strain differentiation among clinical isolates ofPseudomonas aeruginosa,and to compare this technique with the traditional gel method for DNA separation.Methods:One hundred clinical strains ofP. aeruginosaobtained from a hospital in northwestern Ohio were tested for reactivity to 3 serotype-specific monoclonal antibodies by enzyme-linked immunosorbent assay. Twelve strains (4 from each serogroup) were selected for DNA analysis by polymerase chain reaction (PCR)-based, single primer DNA fingerprinting methods with 3 different primers: 1 enterobacterial repetitive intergenic consensus PCR and 2 arbitrarily primed PCRs. The PCR products were analyzed by agarose slab gel and microchip gel electrophoresis.Results:Of the 100 clinical isolates tested, 39% (4%, 14%, and 21%) were found to be serotypes 0:3, 0:6, and 0:11, respectively. Twelve strains were chosen for DNA analysis by PCR. The PCR products were analyzed by agarose slab gel electrophoresis and on microchips to determine interspecies diversity. Both methods demonstrated that different serotypes exhibited different electrophoretic patterns. Two strains (clinical strains 6 and 7, serotype 0:6) showed identical patterns, indicating a high degree of relatedness.Conclusion:In all cases, there was concordance between the electrophoretic patterns detected by the two methods. The capability of conducting both PCR and microchip gel electrophoresis offers an opportunity for an automated and rapid method for genetic analysis and differentiation among strains ofP. aeruginosaand other microorganisms.

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32

Izhberdeeva, Margarita P., Anastasiya A. Sautkina, Irina A. Barkova, and Dmitry V. Viktorov. "Antigenic identity of immunodominant proteins of <i>Bacillus anthracis</i> genovariants." Journal of microbiology, epidemiology and immunobiology 100, no. 2 (May 22, 2023): 203–8. http://dx.doi.org/10.36233/0372-9311-284.

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Introduction. The main biological raw materials for the production of immunobiological preparations for identification of Bacillus anthracis are its specific antigens, the protective antigen and the EA1 protein. Purpose. To determine the antigenic identity of immunodominant proteins of different genovariants of B. anthracis isolated by gel chromatography and electrophoresis. Materials and methods. Culture filtrates of isogenic variants of B. anthracis strain 575/122 (pXO1+, pXO2+): R01 (pXO1+, pXO2); R00 (pXO1, pXO2) were used in the study. Gel chromatographic fractionation and electrophoretic separation were carried out according to standard methods. The antigenic properties of proteins isolated by gel chromatography and electrophoresis were studied by immunodiffusion with polyclonal monospecific sera against the protective antigen and the EA1 protein of the S-layer. Results. Gel chromatographic separation of B. anthracis 575/122 culture filtrates R01 (pXO1+, pXO2) and R00 (pXO1, pXO2)yielded fractions 1 and 5. Sera against EA1 protein and antigens of fraction 1 of strains B. anthracis 575/122 R00 and B. anthracis 575/122 R01 culture filtrates identified the identical antigens. Serum against antigens of fraction 5 of B. anthracis 575/122 R01 contained antibodies to numerous proteins, including the protective antigen isolated by electrophoresis. Discussion. The antigenic identity of immunodominant proteins isolated by gel chromatography and electrophoresis was identified. Conclusion. EA1 and PA proteins isolated by electrophoresis and gel chromatography can be used for production of monoclonal and polyclonal monospecific antibodies suitable for the design of diagnostic preparations.

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33

Munro, Nicole J., Karen Snow, Jeffrey A. Kant, and James P. Landers. "Molecular Diagnostics on Microfabricated Electrophoretic Devices: From Slab Gel- to Capillary- to Microchip-based Assays for T- and B-Cell Lymphoproliferative Disorders." Clinical Chemistry 45, no. 11 (November 1, 1999): 1906–17. http://dx.doi.org/10.1093/clinchem/45.11.1906.

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Abstract Background: Current methods for molecular-based diagnosis of disease rely heavily on modern molecular biology techniques for interrogating the genome for aberrant DNA sequences. These techniques typically include amplification of the target DNA sequences followed by separation of the amplified fragments by slab gel electrophoresis. As a result of the labor-intensive, time-consuming nature of slab gel electrophoresis, alternative electrophoretic formats have been developed in the form of capillary electrophoresis and, more recently, multichannel microchip electrophoresis. Methods: Capillary electrophoresis was explored as an alternative to slab gel electrophoresis for the analysis of PCR-amplified products indicative of T- and B-cell malignancies as a means of defining the elements for silica microchip-based diagnosis. Capillary-based separations were replicated on electrophoretic microchips. Results: The microchip-based electrophoretic separation effectively resolved PCR-amplified fragments from the variable region of the T-cell receptor-γ gene (150–250 bp range) and the immunoglobulin heavy chain gene (80–140 bp range), yielding diagnostically relevant information regarding the presence of clonal DNA populations. Although hydroxyethylcellulose provided adequate separation power, the need for a coated microchannel for effective resolution necessitated additional preparative steps. In addition, preliminary data are shown indicating that polyvinylpyrrolidone may provide an adequate matrix without the need for microchannel coating. Conclusions: Separation of B- and T-cell gene rearrangement PCR products on microchips provides diagnostic information in dramatically reduced time (160 s vs 2.5 h) with no loss of diagnostic capacity when compared with current methodologies. As illustrated, this technology and methodology holds great potential for extrapolation to the abundance of similar molecular biology-based techniques.

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Balogun, Kayode, Megan Lee, and Kelly Doyle. "Comparison of Heat Fractionation and Gel Electrophoresis Methods for the Quantitative Determination of Alkaline Phosphatase Isoenzymes." American Journal of Clinical Pathology 154, Supplement_1 (October 2020): S8. http://dx.doi.org/10.1093/ajcp/aqaa137.014.

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Abstract Introduction Alkaline phosphatase (ALP) is important in the diagnostic work-up for hepatobiliary and bone diseases. ALP isoenzymes are expressed in the bone, liver, kidney, placenta, and intestine, and vary in heat stability and electrophoretic mobility. Distinguishing the different ALP isoenzymes is clinically important for the diagnosis of pathologies associated with elevated ALP activity. Current modalities available to measure ALP isoenzymes utilize the heat stability, electrophoretic mobility, and immunochemical properties of the isoenzymes. The differences inherent in these methods allow for unique benefits of each method in identifying ALP isoenzymes. The objective of this study was to compare bone, liver, and placental ALP isoenzyme results determined by heat fractionation and gel electrophoresis and to characterize the heat-stable non-liver fraction (t1/2 >11 min), reported by heat fractionation, using gel electrophoresis. Methods A total of 72 de-identified serum samples that span a wide range of known ALP isoenzyme concentrations and disease states were used to measure ALP using gel electrophoresis and heat fractionation. Heat fractionation was achieved by selective inactivation of the isoenzymes at 56 °C in 10, 15, and 20-minute intervals. Log-percent activity of the total and heat-inactivated fractions at each time point was plotted against time in minutes. The linear activity decay between 10 and 20 minutes determined the relative amount of liver isoenzyme activity and the slope of the line determined the half-lives of ALP isoenzymes. Electrophoresis was performed according to the manufacturer’s protocol using the Hydragel ISO-PAL gel to resolve ALP isoenzymes based on their electrophoretic mobility and interaction with lectin. ALP isoenzymes were quantified by densitometry. Results Our results show a significant correlation coefficient (r) of 0.98, Deming regression slope of 1.1, and bias of -1.2% for the liver isoenzyme (n=43). However, liver fractions are not distinguishable by heat fractionation when heat-stable isoforms are present. The bone fraction (n=43) showed a coefficient of correlation of 0.86, slope of 0.55, and bias of -31%. Although, with a small sample size (n=6), the placental isoenzyme showed a significant agreement between the two methods: r = 0.999, slope = 0.98, and a -3.5% bias. Of the non-liver fractions reported by heat fractionation (n=13, ALP >100 U/L) eleven (85%) showed distinct qualitative bands in the intestinal lane on gel electrophoresis; however, quantitative values did not correlate between the two methods. Conclusion Our data support an agreement between the heat fractionation and gel electrophoresis methods for the quantitative determination of liver and placental alkaline phosphatase isoenzymes. Although there is an association between the two methods, the activity of the bone isoenzyme was underestimated by the gel electrophoresis method, likely due to saturation of the gel and densitometry scan because of elevated protein concentrations. The non-liver fractions were qualitatively identified as intestinal isoenzyme.

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35

Green, Michael R., and Joseph Sambrook. "Alkaline Agarose Gel Electrophoresis." Cold Spring Harbor Protocols 2021, no. 11 (November 2021): pdb.prot100438. http://dx.doi.org/10.1101/pdb.prot100438.

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Alkaline agarose gels are run at high pH, which causes each thymine and guanine residue to lose a proton and thus prevents the formation of hydrogen bonds with their adenine and cytosine partners. The denatured DNA is maintained in a single-stranded state and migrates through an alkaline agarose gel as a function of its size. Other denaturants such as formamide and urea do not work well because they cause the agarose to become rubbery.

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36

Shaffer, Edward O. II, and Monica Olvera de la Cruz. "Dynamics of gel electrophoresis." Macromolecules 22, no. 3 (May 1989): 1351–55. http://dx.doi.org/10.1021/ma00193a057.

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37

Ünlü, M. "Title: Difference Gel Electrophoresis." Biochemical Society Transactions 27, no. 3 (June 1, 1999): A67. http://dx.doi.org/10.1042/bst027a067b.

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38

Barlow, Denise. "Pulsed-field gel electrophoresis." Genome 31, no. 1 (January 1, 1989): 465–66. http://dx.doi.org/10.1139/g89-084.

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39

Jones, P. "Gel Electrophoresis. Nucleic Acids." Journal of Steroid Biochemistry and Molecular Biology 64, no. 5-6 (March 1998): 314–15. http://dx.doi.org/10.1016/s0960-0760(96)00242-7.

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40

Gardiner, Katheleen. "Pulsed field gel electrophoresis." Analytical Chemistry 63, no. 7 (April 1991): 658–65. http://dx.doi.org/10.1021/ac00007a003.

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41

Anand, C. V. "Gel electrophoresis: Nucleic acids." Biochemical Education 26, no. 1 (January 1998): 97. http://dx.doi.org/10.1016/s0307-4412(98)00068-5.

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Maizel, Jr, J. "SDS polyacrylamide gel electrophoresis." Trends in Biochemical Sciences 25, no. 12 (December 1, 2000): 590–92. http://dx.doi.org/10.1016/s0968-0004(00)01693-5.

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Boots, Sharon. "Gel electrophoresis of DNA." Analytical Chemistry 61, no. 8 (April 15, 1989): 551A—553A. http://dx.doi.org/10.1021/ac00183a002.

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Baba, Yoshinobu. "Capillary affinity gel electrophoresis." Molecular Biotechnology 6, no. 2 (October 1996): 143–53. http://dx.doi.org/10.1007/bf02740769.

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Mendoza, Llyza, Thilina Gunawardhana, Warren Batchelor, and Gil Garnier. "Nanocellulose for gel electrophoresis." Journal of Colloid and Interface Science 540 (March 2019): 148–54. http://dx.doi.org/10.1016/j.jcis.2019.01.017.

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Wood, EJ. "Gel electrophoresis of proteins." Biochemical Education 21, no. 4 (October 1993): 225–26. http://dx.doi.org/10.1016/0307-4412(93)90119-k.

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Palmer, A. D. "SDS-polyacrylamide gel electrophoresis." Biochemical Education 23, no. 4 (October 1995): 220. http://dx.doi.org/10.1016/0307-4412(95)90169-8.

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Rosenbaum, Volker, and Detlev Riesner. "Temperature-gradient gel electrophoresis." Biophysical Chemistry 26, no. 2-3 (May 1987): 235–46. http://dx.doi.org/10.1016/0301-4622(87)80026-1.

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Spencer, N. "Gel electrophoresis of proteins." FEBS Letters 230, no. 1-2 (March 28, 1988): 221–22. http://dx.doi.org/10.1016/0014-5793(88)80684-7.

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Maule, John. "Pulsed-field gel electrophoresis." Molecular Biotechnology 9, no. 2 (April 1998): 107–26. http://dx.doi.org/10.1007/bf02760813.

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