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Journal articles on the topic 'Apolipoprotein B-100'

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Published: 4 June 2021

Last updated: 8 February 2022

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1

Welty, Francine K., Alice H. Lichtenstein, P. Hugh R. Barrett, Gregory G. Dolnikowski, Jose M. Ordovas, and Ernst J. Schaefer. "Decreased Production and Increased Catabolism of Apolipoprotein B-100 in Apolipoprotein B-67/B-100 Heterozygotes." Arteriosclerosis, Thrombosis, and Vascular Biology 17, no. 5 (May 1997): 881–88. http://dx.doi.org/10.1161/01.atv.17.5.881.

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2

Herbert, P. N., J. S. Hyams, D. N. Bernier, M. M. Berman, A. L. Saritelli, K. M. Lynch, A. V. Nichols, and T. M. Forte. "Apolipoprotein B-100 deficiency. Intestinal steatosis despite apolipoprotein B-48 synthesis." Journal of Clinical Investigation 76, no. 2 (August 1, 1985): 403–12. http://dx.doi.org/10.1172/jci111986.

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3

Edge, Stephen B., Jeffrey M. Hoeg, Philip D. Schneider, and H. Bryan Brewer. "Apolipoprotein B synthesis in humans: Liver synthesizes only apolipoprotein B-100." Metabolism 34, no. 8 (August 1985): 726–30. http://dx.doi.org/10.1016/0026-0495(85)90022-8.

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4

Huet, G., M. C. Dieu, A. Martin, G. Grard, J. M. Bard, P. Fossati, and P. Degand. "Heterozygous hypobetalipoproteinemia with fasting chylomicronemia." Clinical Chemistry 37, no. 2 (February 1, 1991): 296–300. http://dx.doi.org/10.1093/clinchem/37.2.0296.

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Abstract We describe a disorder in which low-density lipoprotein (LDL)-cholesterol and apolipoprotein B are in low concentration (0.47 mmol/L and 0.28 g/L, respectively) and chylomicrons are still present in plasma after an 18-h fast. The d less than 1.006 fraction was isolated by flotation ultracentrifugation and the apolipoproteins were analyzed by electrophoresis, immunoblotting with anti-apolipoprotein B-100 antiserum, and isoelectric focusing. In the d less than 1.006 fraction of the fasting serum, we found an apolipoprotein B form with the same apparent molecular mass as apolipoprotein B-48 and similar in amount to apolipoprotein B-100 (respective percentages, 46% and 54%). The monosialylated form of the apolipoprotein C-III was severely decreased. After an oral fat load, the repartition of the two species of apolipoprotein B did not change greatly (respective percentages, 60% and 40%), and the concentration of serum triglyceride increased only from 1.20 to 1.65 mmol/L.

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5

Chulkova, T. M., and V. V. Tertov. "Degradation of human apolipoprotein B-100 by apolipoprotein(a)." FEBS Letters 336, no. 2 (December 27, 1993): 327–29. http://dx.doi.org/10.1016/0014-5793(93)80830-n.

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6

Schaefer, Juergen R., Hubert Scharnagl, Manfred W. Baumstark, Horst Schweer, Loren A. Zech, Hansjörg Seyberth, Karl Winkler, Armin Steinmetz, and Winfried März. "Homozygous Familial Defective Apolipoprotein B-100." Arteriosclerosis, Thrombosis, and Vascular Biology 17, no. 2 (February 1997): 348–53. http://dx.doi.org/10.1161/01.atv.17.2.348.

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7

Decroli, Eva. "KADAR APOLIPOPROTEIN B 100 SERUM PADA PENDERITA NEFROPATI DIABETIKUM." Majalah Kedokteran Andalas 38, no. 2 (December 8, 2015): 99. http://dx.doi.org/10.22338/mka.v38.i2.p99-107.2015.

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AbstrakPenelitian ini bertujuan untuk mengetahui kadar Apolipoprotein B 100 serum pada penderita nefropati diabetikum. Metode penelitian ini dengan desain cross sectional yang bersifat deskriptif analitik. Populasi adalah semua pasien yang menderita diabetes mellitus tipe 2 yang dirawat di bagian penyakit dalam atau kontrol ke poliklinik khusus metabolik endokrin RSU Dr. M. Djamil Padang. Sampel penelitian adalah pasien diabetes mellitus tipe 2 dengan proteinuria positif yang memenuhi kriteria inklusi dan ekslusi yang diambil secara konsekutif. Sampel penelitian diambil dari darah vena dalam keadaaan puasa selama 12 jam. Pemeriksaan apolipoprotein B 100 serum dilakukan di laboratorium klinik swasta, dengan menggunakan metode imunoturbidimetri. Albumin creatinin ratio merupakan perbandingan kadar albumin urin terhadap kreatinin urin dengan metode pemeriksaan imunoturbidimetri. Pada penelitian ini didapatkan rerata kadar Apolipoprotein B 100 serum yaitu 86,10 mg/dl (nilai normal 66-101 mg/dl) dengan standar deviasi 27,997. Simpulan: Tidak terdapat peningkatan kadar apolipoprotein B 100 serum pada penderita nefropati diabetikum.AbstractThis study aims to examine Apolipoprotein B 100 serum level in diabetic nephropathy patient. Study design was cross sectional with analytic descriptive. Population is all type 2 diabetes mellitus inpatient and outpatient in internal medicine M Djamil hospital. Sample is all type 2 diabetes mellitus consecutive patient with positive proteinuria and fullfilled inclusion and exclusion criteria. Vein blood was taken after 12 hours-fasting. Apolipoprotein B 100 serum check at non-governmental laboratory by immunoturbidimetry methode. Albumin creatinin ratio check by immunoturbidimetry methode. Result: Apolipoprotein B 100 serum level is 86.10 mg/dl (normal value 66-101 mg/dl) with standar deviation 27.997. Conclusion: There is no significant enhancement of apolipoprotein B 100 serum level in diabetic nephropathy patient.

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8

Innerarity, TL, RW Mahley, KH Weisgraber, TP Bersot, RM Krauss, GL Vega, SM Grundy, W. Friedl, J. Davignon, and BJ McCarthy. "Familial defective apolipoprotein B-100: a mutation of apolipoprotein B that causes hypercholesterolemia." Journal of Lipid Research 31, no. 8 (August 1990): 1337–49. http://dx.doi.org/10.1016/s0022-2275(20)42605-7.

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9

Soria, L. F., E. H. Ludwig, H. R. Clarke, G. L. Vega, S. M. Grundy, and B. J. McCarthy. "Association between a specific apolipoprotein B mutation and familial defective apolipoprotein B-100." Proceedings of the National Academy of Sciences 86, no. 2 (January 1, 1989): 587–91. http://dx.doi.org/10.1073/pnas.86.2.587.

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10

Chen, G. C., S. Zhu, D. A. Hardman, J. W. Schilling, K. Lau, and J. P. Kane. "Structural Domains of Human Apolipoprotein B-100." Journal of Biological Chemistry 264, no. 24 (August 1989): 14369–75. http://dx.doi.org/10.1016/s0021-9258(18)71687-6.

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11

Weisgraber, K. H., and S. C. Rall. "Human apolipoprotein B-100 heparin-binding sites." Journal of Biological Chemistry 262, no. 23 (August 1987): 11097–103. http://dx.doi.org/10.1016/s0021-9258(18)60931-7.

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12

Ng, Theodore WK, Esther MM Ooi, Gerald F. Watts, Dick C. Chan, and P. Hugh R. Barrett. "Genetic determinants of apolipoprotein B-100 kinetics." Current Opinion in Lipidology 21, no. 2 (April 2010): 141–47. http://dx.doi.org/10.1097/mol.0b013e3283378e5a.

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13

Ladias, John A. A. "Apolipoprotein B-100 Hopkins (Arginine4019 [unk] Tryptophan)." JAMA 262, no. 14 (October 13, 1989): 1980. http://dx.doi.org/10.1001/jama.1989.03430140098032.

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14

Gašparovič, Juraj, Zuzana Bašistová, L’ubomíra Fábryová, Ladislava Wsólová, Branislav Vohnout, and Katarína Rašlová. "Familial defective apolipoprotein B-100 in Slovakia." Atherosclerosis 194, no. 2 (October 2007): e95-e107. http://dx.doi.org/10.1016/j.atherosclerosis.2006.10.015.

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15

Andersen, Lars H., André R. Miserez, Zahid Ahmad, and Rolf L. Andersen. "Familial defective apolipoprotein B-100: A review." Journal of Clinical Lipidology 10, no. 6 (November 2016): 1297–302. http://dx.doi.org/10.1016/j.jacl.2016.09.009.

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16

Hospattankar, A. V., T. Fairwell, M. Meng, R. Ronan, and H. B. Brewer. "Identification of sequence homology between human plasma apolipoprotein B-100 and apolipoprotein B-48." Journal of Biological Chemistry 261, no. 20 (July 1986): 9102–4. http://dx.doi.org/10.1016/s0021-9258(18)67622-7.

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17

Johs, Alexander, Michal Hammel, Ines Waldner, Roland P. May, Peter Laggner, and Ruth Prassl. "Modular Structure of Solubilized Human Apolipoprotein B-100." Journal of Biological Chemistry 281, no. 28 (May 16, 2006): 19732–39. http://dx.doi.org/10.1074/jbc.m601688200.

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18

Mashima, Ryuichi, Shinichi Yoshimura, and Yorihiro Yamamoto. "Reduction of Lipid Hydroperoxides by Apolipoprotein B-100." Biochemical and Biophysical Research Communications 259, no. 1 (May 1999): 185–89. http://dx.doi.org/10.1006/bbrc.1999.0739.

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19

Madsen, Eva M., Marie L. S. Lindegaard, Claus B. Andersen, Peter Damm, and Lars B. Nielsen. "Human Placenta Secretes Apolipoprotein B-100-containing Lipoproteins." Journal of Biological Chemistry 279, no. 53 (October 25, 2004): 55271–76. http://dx.doi.org/10.1074/jbc.m411404200.

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20

Lee, Diana M., and Shyam Singh. "Degradation of apolipoprotein B-100 in human chylomicrons." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 960, no. 2 (May 1988): 148–56. http://dx.doi.org/10.1016/0005-2760(88)90060-4.

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21

Abdel-Wareth, Laila O., Simon N. Pimstone, Jean-Pierre Lagarde, Alain Raisonnier, Pascale Benlian, Haydn Pritchard, Michael R. Hayden, and Jiri J. Frohlich. "Familial defective apolipoprotein B-100 in hypercholesterolemic Chinese Canadians: identification of a unique haplotype of the apolipoprotein B-100 allele." Atherosclerosis 135, no. 2 (December 1997): 181–85. http://dx.doi.org/10.1016/s0021-9150(97)00159-7.

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22

Ladias, J. A. "Apolipoprotein B-100 Hopkins (arginine4019----tryptophan). A new apolipoprotein B-100 variant in a family with premature atherosclerosis and hyperapobetalipoproteinemia." JAMA: The Journal of the American Medical Association 262, no. 14 (October 13, 1989): 1980–88. http://dx.doi.org/10.1001/jama.262.14.1980.

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23

Windler, E. E. T., J. Greeve, W. H. Daerr, and H. Greten. "Binding of rat chylomicrons and their remnants to the hepatic low-density-lipoprotein receptor and its role in remnant removal." Biochemical Journal 252, no. 2 (June 1, 1988): 553–61. http://dx.doi.org/10.1042/bj2520553.

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Binding and uptake of rat chylomicrons of different metabolic stages by the hepatic low-density-lipoprotein (LDL) receptor were studied. Pure chylomicrons, characterized by apolipoprotein B-48 devoid of contaminating B-100, were labelled in their cholesteryl esters. Lymph chylomicrons and serum chylomicrons, enriched in apolipoprotein E and the C-apolipoproteins, bound poorly to rat hepatic membranes. In contrast, chylomicron remnants, containing the apolipoproteins B-48 and E, bound with high affinity. Specific binding of remnants was virtually completely competed for by LDL free of apolipoprotein E. In addition, in ligand blots both remnants and LDL associated with the same protein with an Mr characteristic of the LDL receptor. Uptake of remnants during a single pass through isolated perfused rat livers was decreased to about 50% by an excess of LDL. It is concluded that rat chylomicron remnants are a ligand of the hepatic LDL receptor. The much higher affinity as compared with LDL is mediated by apolipoprotein E but not B-48, and is inhibited by the C-apolipoproteins. This explains why serum chylomicrons are not taken up by the liver, whereas remnants are rapidly removed from the circulation. Results from experiments in vivo suggest that the LDL receptor makes an important contribution to the hepatic uptake of remnants and may be the principal binding site of the liver responsible for remnant removal.

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24

Zlot, Constance H., Laura M. Flynn, Murielle M. Véniant, Edward Kim, Martin Raabe, Sally P. A. McCormick, Patricia Ambroziak, Leslie M. McEvoy, and Stephen G. Young. "Generation of monoclonal antibodies specific for mouse apolipoprotein B-100 in apolipoprotein B-48-only mice." Journal of Lipid Research 40, no. 1 (January 1999): 76–84. http://dx.doi.org/10.1016/s0022-2275(20)33341-1.

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25

Demant, T., D. Bedford, C. J. Packard, and J. Shepherd. "Influence of apolipoprotein E polymorphism on apolipoprotein B-100 metabolism in normolipemic subjects." Journal of Clinical Investigation 88, no. 5 (November 1, 1991): 1490–501. http://dx.doi.org/10.1172/jci115459.

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26

Peel, Andrew S., Antonios Zampelas, Christine M. Williams, and Barry J. Gould. "A Novel Antiserum Specific to Apolipoprotein B-48: Application in the Investigation of Postprandial Lipidaemia in Humans." Clinical Science 85, no. 5 (November 1, 1993): 521–24. http://dx.doi.org/10.1042/cs0850521.

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1. Apolipoprotein B-48, the transport protein for chylomicrons, is identical with apolipoprotein B-100 for the first 48% of its sequence. No antiserum has yet been reported that can recognize apolipoprotein B-48, but not apolipoprotein B-100. 2. In the present study an antiserum was raised to the C-terminal sequence of apolipoprotein B-48, using specific chemical reactions to ensure that the charged carboxyl group of the C-terminal isoleucine residue was free. In a Western blot the antiserum was shown to bind to a protein band having the characteristics of apolipoprotein B-48, but not to apolipoprotein B-100. 3. In the early evening 11 subjects were given a test meal which contained 40 g of mixed oil and retinyl palmitate. Blood samples were collected over 9 h. Chylomicron-enriched fractions were prepared and analysed for triacylglycerol, retinyl palmitate and apolipoprotein B-48, the latter after separation using SDS/PAGE and visualization by chemiluminescence on a Western blot. Both triacylglycerol and apolipoprotein B-48 showed an early peak at 1 h, which was not seen with retinyl palmitate. All three substances gave a broader peak between 5 and 6 h post-prandially. Retinyl palmitate concentrations declined rapidly during the late (6-9 h) postprandial period, but apolipoprotein B-48 concentrations remained elevated. 4. This study has shown that an antiserum has been produced which is specific for apolipoprotein B-48. This has enabled measurement of postprandial concentrations of the protein that revealed features of chylomicron metabolism which have not been reported previously.

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27

Welty, Francine K., Alice H. Lichtenstein, P. Hugh R. Barrett, Gregory G. Dolnikowski, and Ernst J. Schaefer. "Interrelationships Between Human Apolipoprotein A-I and Apolipoproteins B-48 and B-100 Kinetics Using Stable Isotopes." Arteriosclerosis, Thrombosis, and Vascular Biology 24, no. 9 (September 2004): 1703–7. http://dx.doi.org/10.1161/01.atv.0000137975.14996.df.

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28

Delporte, C., P. Van Antwerpen, K. Zouaoui Boudjeltia, C. Noyon, D. Calay, F. Reyé, A. Rousseau, et al. "P353 SPECIFIC OXIDATION OF APOLIPOPROTEIN-B-100 BY MYELOPEROXIDASE." Atherosclerosis Supplements 11, no. 2 (June 2010): 91–92. http://dx.doi.org/10.1016/s1567-5688(10)70420-7.

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29

Fraza, L. W. L., K. A. Ankone, M. Anker, G. C. G. van Rijckevorsel, C. L. Pricker, J. C. Defesche, and J. J. P. Kastelein. "Familial defective apolipoprotein B-100: one hundred Dutch heterozygotes." Atherosclerosis 109, no. 1-2 (September 1994): 205. http://dx.doi.org/10.1016/0021-9150(94)93823-7.

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30

Maher, VincentM G., JohnJ Gallagher, GilbertR Thompson, and NicholasB Myant. "Cholesterol-lowering drugs in familial defective apolipoprotein B-100." Lancet 339, no. 8796 (March 1992): 811. http://dx.doi.org/10.1016/0140-6736(92)91939-6.

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31

Segrest, Jere P., Martin K. Jones, Hans De Loof, and Nassrin Dashti. "Structure of apolipoprotein B-100 in low density lipoproteins." Journal of Lipid Research 42, no. 9 (September 2001): 1346–67. http://dx.doi.org/10.1016/s0022-2275(20)30267-4.

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32

Zulewski, Henryk, Ron Ninnis, André R. Miserez, Manfred W. Baumstark, and Ulrich Keller. "VLDL and IDL apolipoprotein B-100 kinetics in familial hypercholesterolemia due to impaired LDL receptor function or to defective apolipoprotein B-100." Journal of Lipid Research 39, no. 2 (February 1998): 380–87. http://dx.doi.org/10.1016/s0022-2275(20)33899-2.

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33

Chan, Dick C., Gerald F. Watts, Trevor G. Redgrave, Trevor A. Mori, and P. Hugh R. Barrett. "Apolipoprotein B-100 kinetics in visceral obesity: Associations with plasma apolipoprotein C-III concentration." Metabolism 51, no. 8 (August 2002): 1041–46. http://dx.doi.org/10.1053/meta.2002.33339.

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34

de Silva, H. V., J. Más-Oliva, J. M. Taylor, and R. W. Mahley. "Identification of apolipoprotein B-100 low density lipoproteins, apolipoprotein B-48 remnants, and apolipoprotein E-rich high density lipoproteins in the mouse." Journal of Lipid Research 35, no. 7 (July 1994): 1297–310. http://dx.doi.org/10.1016/s0022-2275(20)39973-9.

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35

Yang, CY, ZW Gu, N. Valentinova, HJ Pownall, B. Lee, M. Yang, YH Xie, JR Guyton, TN Vlasik, and JC Fruchart. "Human very low density lipoprotein structure: interaction of the C apolipoproteins with apolipoprotein B-100." Journal of Lipid Research 34, no. 8 (August 1993): 1311–21. http://dx.doi.org/10.1016/s0022-2275(20)36961-3.

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36

Miserez, A. R., R. Laager, N. Chiodetti, and U. Keller. "High prevalence of familial defective apolipoprotein B-100 in Switzerland." Journal of Lipid Research 35, no. 4 (April 1994): 574–83. http://dx.doi.org/10.1016/s0022-2275(20)41171-x.

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37

Kivlen, M. H., C. A. Dorsey, V. R. Lingappa, and R. S. Hegde. "Asymmetric distribution of pause transfer sequences in apolipoprotein B-100." Journal of Lipid Research 38, no. 6 (June 1997): 1149–62. http://dx.doi.org/10.1016/s0022-2275(20)37197-2.

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38

Chen, G. Chi, David A. Hardman, Robert L. Hamilton, Carl M. Mendel, James W. Schilling, Shan Zhu, Kenneth Lau, Jinny S. Wong, and John P. Kane. "Distribution of lipid-binding regions in human apolipoprotein B-100." Biochemistry 28, no. 6 (March 1989): 2477–84. http://dx.doi.org/10.1021/bi00432a019.

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39

Véniant, M. "Lipoproteins Containing Apolipoprotein B-100 Are Secreted by the Heart." Trends in Cardiovascular Medicine 9, no. 3-4 (May 1999): 103–7. http://dx.doi.org/10.1016/s1050-1738(99)00011-0.

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40

Levy, E., C. Rochette, I. Londono, CC Roy, RW Milne, YL Marcel, and M. Bendayan. "Apolipoprotein B-100: immunolocalization and synthesis in human intestinal mucosa." Journal of Lipid Research 31, no. 11 (November 1990): 1937–46. http://dx.doi.org/10.1016/s0022-2275(20)42258-8.

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41

Bednarska-Makaruk, M., M. Bisko, M. F. Puławska, D. Hoffman-Zacharska, M. Rodo, M. Roszczynko, A. Solik-Tomassi, et al. "Familial defective apolipoprotein B-100 in hypercholesterolemic patients in Poland." Atherosclerosis 151, no. 1 (July 2000): 322. http://dx.doi.org/10.1016/s0021-9150(00)81469-0.

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42

TAMURA, MICHIRO, AKIRA TANAKA, KATSUMASA YUI, FUJIO NUMANO, KATSUYUKI NAKAJIMA, HANA HIYAMIZU, and NORIKO KATSUTA. "Presence of Apolipoprotein B-100 in Human Intestine Epithelial Cells." Annals of the New York Academy of Sciences 811, no. 1 Atheroscleros (April 1997): 488–92. http://dx.doi.org/10.1111/j.1749-6632.1997.tb52030.x.

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43

Yang, C. Y., Z. W. Gu, S. A. Weng, T. W. Kim, S. H. Chen, H. J. Pownall, P. M. Sharp, S. W. Liu, W. H. Li, and A. M. Gotto. "Structure of apolipoprotein B-100 of human low density lipoproteins." Arteriosclerosis: An Official Journal of the American Heart Association, Inc. 9, no. 1 (January 1989): 96–108. http://dx.doi.org/10.1161/01.atv.9.1.96.

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44

ITOH, Hiroshi, Keiji TAMURA, Yoshiko MOTOI, and Fumio KAWAWA. "Serum Apolipoprotein B-100 Concentrations in Healthy and Diseased Cattle." Journal of Veterinary Medical Science 59, no. 7 (1997): 587–91. http://dx.doi.org/10.1292/jvms.59.587.

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45

Wada, Y., S. Matsubara, J. Dufresne, GM Hargrove, ZF Stephan, RE Steele, and NC Wong. "Effects of a thyromimetic on apolipoprotein B-100 in rats." Journal of Molecular Endocrinology 25, no. 3 (December 1, 2000): 299–308. http://dx.doi.org/10.1677/jme.0.0250299.

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We have studied the effects of a cardiac sparing thyromimetic, CGS 23425, on postprandial levels of triglycerides, abundance of apolipoprotein B (apo B) protein and hepatic apo B mRNA expression in rats. When compared with control rats, triglyceride clearance was significantly accelerated by treatment with CGS 23425. A full return to baseline values was achieved within 8 h after ingesting a large quantity of fat, as compared to >24 h in control animals. The abundance of apo B-100 protein in CGS 23425-treated hyperlipidemic rats decreased in a dose-dependent manner, but levels of apo B-48 were not significantly affected. Like L-tri-iodothyronine (L-T(3)), treatment with 30 microg/kg CGS 23425 for 6 or 9 days decreased the levels of apo B-100 protein by 80% and 40% respectively. This change was paralleled by a 27% reduction in hepatic apo B-100 mRNA. To investigate a potential mechanism of CGS 23425 action, we measured in vitro apo B mRNA editing activity in hepatocellular extract from control or CGS 23425-treated rats. Treatment with CGS 23425 increased activity of the hepatic apo B-100 editosome, apobec-1. In human hepatoma cells which lack apobec-1 activity, apo B-100 mRNA levels remained the same in cells treated with or without the agent. In summary, these observations show that CGS 23425 decreases the levels of apo B-100 in rats. This action of CGS 23425 involves apo B-100 mRNA editing activity.

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46

Mittal, Balraj, Mahendra Kumar Singh, Udai Bhan Pandey, Uday Chand Ghoshal, Itha Srivenu, Vinay Kumar Kapoor, and Gourdas Choudhuri. "Apolipoprotein B-100 Xba I gene polymorphism in gallbladder cancer." Human Genetics 114, no. 3 (February 1, 2004): 280–83. http://dx.doi.org/10.1007/s00439-003-1056-8.

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47

Illingworth, D. R., F. Vakar, R. W. Mahley, and K. H. Weisgraber. "Hypocholesterolaemic effects of lovastatin in familial defective apolipoprotein B-100." Lancet 339, no. 8793 (March 1992): 598–600. http://dx.doi.org/10.1016/0140-6736(92)90875-4.

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48

Cardin, Alan D., and Richard L. Jackson. "Interaction of tryptic peptides of apolipoprotein B-100 with dimyristoylphosphatidylcholine." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 877, no. 3 (July 1986): 366–71. http://dx.doi.org/10.1016/0005-2760(86)90201-8.

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49

Andersen, Lars H., Rolf L. Andersen, and André R. Miserez. "Familial defective apolipoprotein B-100: a tale of twin mutations." Journal of Clinical Lipidology 10, no. 4 (July 2016): 1050–51. http://dx.doi.org/10.1016/j.jacl.2016.04.007.

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50

Cruzado, Ingrid D., Steven L. Cockrill, Catherine J. McNeal, and Ronald D. Macfarlane. "Characterization and quantitation of apolipoprotein B-100 by capillary electrophoresis." Journal of Lipid Research 39, no. 1 (January 1998): 205–17. http://dx.doi.org/10.1016/s0022-2275(20)34216-4.

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