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The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins.

The Biochemical journal

Adair GS, Robinson ME.
PMID: 16744543
Biochem J. 1930;24(6):1864-89. doi: 10.1042/bj0241864.

No abstract available.

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Adair GS, Robinson ME. The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins. Biochem J. 1930;24(6):1864-89doi: 10.1042/bj0241864.
Adair, G. S., & Robinson, M. E. (1930). The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins. The Biochemical journal, 24(6), 1864-89. https://doi.org/10.1042/bj0241864
Adair, G S, and Robinson, M E. "The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins." The Biochemical journal vol. 24,6 (1930): 1864-89. doi: https://doi.org/10.1042/bj0241864
Adair GS, Robinson ME. The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins. Biochem J. 1930;24(6):1864-89. doi: 10.1042/bj0241864. PMID: 16744543; PMCID: PMC1254808.
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Influence of Sulfur Nutrition on Developmental Patterns of Some Major Pea Seed Proteins and Their mRNAs.

Plant physiology

Chandler PM, Spencer D, Randall PJ, Higgins TJ.
PMID: 16663681
Plant Physiol. 1984 Jul;75(3):651-7. doi: 10.1104/pp.75.3.651.

In addition to the marked reduction in legumin synthesis and legumin mRNA levels reported earlier (Chandler, Higgins, Randall, Spencer 1983 Plant Physiol 71: 47-54), pulse labeling of S-deficient Pisum sativum L. seeds showed that a high relative level of...

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Chandler PM, Spencer D, Randall PJ, et al. Influence of Sulfur Nutrition on Developmental Patterns of Some Major Pea Seed Proteins and Their mRNAs. Plant Physiol. 1984;75(3):651-7doi: 10.1104/pp.75.3.651.
Chandler, P. M., Spencer, D., Randall, P. J., & Higgins, T. J. (1984). Influence of Sulfur Nutrition on Developmental Patterns of Some Major Pea Seed Proteins and Their mRNAs. Plant physiology, 75(3), 651-7. https://doi.org/10.1104/pp.75.3.651
Chandler, P M, et al. "Influence of Sulfur Nutrition on Developmental Patterns of Some Major Pea Seed Proteins and Their mRNAs." Plant physiology vol. 75,3 (1984): 651-7. doi: https://doi.org/10.1104/pp.75.3.651
Chandler PM, Spencer D, Randall PJ, Higgins TJ. Influence of Sulfur Nutrition on Developmental Patterns of Some Major Pea Seed Proteins and Their mRNAs. Plant Physiol. 1984 Jul;75(3):651-7. doi: 10.1104/pp.75.3.651. PMID: 16663681; PMCID: PMC1066970.
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Oxidative hemolysis of erythrocytes.

Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology

Włodek L, Kusior D.
PMID: 21638742
Biochem Mol Biol Educ. 2006 Nov;34(6):438-43. doi: 10.1002/bmb.2006.494034062681.

This exercise for students will allow them to simultaneously observe lipid peroxidation and consequent hemolysis of rat erythrocytes and the effect of sodium azide, a catalase inhibitor, on these processes. It will also demonstrate a protective action of antioxidants,...

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Włodek L, Kusior D. Oxidative hemolysis of erythrocytes. Biochem Mol Biol Educ. 2006;34(6):438-43doi: 10.1002/bmb.2006.494034062681.
Włodek, L., & Kusior, D. (2006). Oxidative hemolysis of erythrocytes. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 34(6), 438-43. https://doi.org/10.1002/bmb.2006.494034062681
Włodek, Lidia, and Kusior, Dorota. "Oxidative hemolysis of erythrocytes." Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology vol. 34,6 (2006): 438-43. doi: https://doi.org/10.1002/bmb.2006.494034062681
Włodek L, Kusior D. Oxidative hemolysis of erythrocytes. Biochem Mol Biol Educ. 2006 Nov;34(6):438-43. doi: 10.1002/bmb.2006.494034062681. PMID: 21638742.
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SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS.

The Journal of experimental medicine

Rothen A, Landsteiner K.
PMID: 19871249
J Exp Med. 1942 Nov 01;76(5):437-50. doi: 10.1084/jem.76.5.437.

Films of several proteins, hen ovalbumin, horse and human serum albumins, and globulins were found to combine specifically with antibodies, showing that the reactions can take place independently of the structure which secures the compact shape of the protein...

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Rothen A, Landsteiner K. SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS. J Exp Med. 1942;76(5):437-50doi: 10.1084/jem.76.5.437.
Rothen, A., & Landsteiner, K. (1942). SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS. The Journal of experimental medicine, 76(5), 437-50. https://doi.org/10.1084/jem.76.5.437
Rothen, A, and Landsteiner, K. "SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS." The Journal of experimental medicine vol. 76,5 (1942): 437-50. doi: https://doi.org/10.1084/jem.76.5.437
Rothen A, Landsteiner K. SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS. J Exp Med. 1942 Nov 01;76(5):437-50. doi: 10.1084/jem.76.5.437. PMID: 19871249; PMCID: PMC2135235.
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Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins.

BMC research notes

Polzer S, van Yperen M, Kirst M, Schwalbe B, Schaal H, Schreiber M.
PMID: 20525179
BMC Res Notes. 2010 Jun 02;3:155. doi: 10.1186/1756-0500-3-155.

BACKGROUND: Myeloperoxidase (MPO), an important element of the microbicidal activity of neutrophils, generates hypochlorous acid (HOCl) from H2O2 and chloride, which is released into body fluids. Besides its direct microbicidal activity, HOCl can react with amino acid residues and...

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Polzer S, van Yperen M, Kirst M, et al. Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins. BMC Res Notes. 2010;3:155doi: 10.1186/1756-0500-3-155.
Polzer, S., van Yperen, M., Kirst, M., Schwalbe, B., Schaal, H., & Schreiber, M. (2010). Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins. BMC research notes, 3155. https://doi.org/10.1186/1756-0500-3-155
Polzer, Svenja, et al. "Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins." BMC research notes vol. 3 (2010): 155. doi: https://doi.org/10.1186/1756-0500-3-155
Polzer S, van Yperen M, Kirst M, Schwalbe B, Schaal H, Schreiber M. Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins. BMC Res Notes. 2010 Jun 02;3:155. doi: 10.1186/1756-0500-3-155. PMID: 20525179; PMCID: PMC2887905.
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Protein adsorption to surface chemistry and crystal structure modification of titanium surfaces.

Journal of oral & maxillofacial research

Jimbo R, Ivarsson M, Koskela A, Sul YT, Johansson CB.
PMID: 24421973
J Oral Maxillofac Res. 2010 Oct 01;1(3):e3. doi: 10.5037/jomr.2010.1303. eCollection 2010.

OBJECTIVES: To observe the early adsorption of extracellular matrix and blood plasma proteins to magnesium-incorporated titanium oxide surfaces, which has shown superior bone response in animal models.MATERIAL AND METHODS: Commercially pure titanium discs were blasted with titanium dioxide (TiO2)...

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Jimbo R, Ivarsson M, Koskela A, et al. Protein adsorption to surface chemistry and crystal structure modification of titanium surfaces. J Oral Maxillofac Res. 2010;1(3):e3doi: 10.5037/jomr.2010.1303.
Jimbo, R., Ivarsson, M., Koskela, A., Sul, Y. T., & Johansson, C. B. (2010). Protein adsorption to surface chemistry and crystal structure modification of titanium surfaces. Journal of oral & maxillofacial research, 1(3), e3. https://doi.org/10.5037/jomr.2010.1303
Jimbo, Ryo, et al. "Protein adsorption to surface chemistry and crystal structure modification of titanium surfaces." Journal of oral & maxillofacial research vol. 1,3 (2010): e3. doi: https://doi.org/10.5037/jomr.2010.1303
Jimbo R, Ivarsson M, Koskela A, Sul YT, Johansson CB. Protein adsorption to surface chemistry and crystal structure modification of titanium surfaces. J Oral Maxillofac Res. 2010 Oct 01;1(3):e3. doi: 10.5037/jomr.2010.1303. eCollection 2010. PMID: 24421973; PMCID: PMC3886052.
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[Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors].

Planta

Miège MN, Mascherpa JM, Royer-Spierer A, Grange A, Miège J.
PMID: 24424699
Planta. 1976 Jan;131(1):81-6. doi: 10.1007/BF00387349.

Cotyledonary cells are submitted to fractionation by isopycnic centrifugation. Small intact protein bodies are collected in the densest zones (d=1.205-1.237 g/cm(3)). Fragments of larger bodies are gathered in zones of lower density (d=1.205 g/cm(3)). Small dense bodies are largely...

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Miège MN, Mascherpa JM, Royer-Spierer A, et al. Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta. 1976;131(1):81-6doi: 10.1007/BF00387349.
Miège, M. N., Mascherpa, J. M., Royer-Spierer, A., Grange, A., & Miège, J. (1976). Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta, 131(1), 81-6. https://doi.org/10.1007/BF00387349
Miège, M N, et al. "Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine." [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta vol. 131,1 (1976): 81-6. doi: https://doi.org/10.1007/BF00387349
Miège MN, Mascherpa JM, Royer-Spierer A, Grange A, Miège J. Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta. 1976 Jan;131(1):81-6. doi: 10.1007/BF00387349. French. PMID: 24424699.
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The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Konarev A.
PMID: 24276390
Theor Appl Genet. 1981 Mar;59(2):117-21. doi: 10.1007/BF00285901.

Immunochemical protein studies show that nongliadins of the ethanol-soluble fraction (EF) provide the best biochemical information on genome interrelations in cereals. After electrophoresis (pH 3.2) these genome specific proteins are shown to fall within the category of α-prolamines and...

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Konarev A. The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. Theor Appl Genet. 1981;59(2):117-21doi: 10.1007/BF00285901.
Konarev, A. (1981). The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 59(2), 117-21. https://doi.org/10.1007/BF00285901
Konarev, A. "The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 59,2 (1981): 117-21. doi: https://doi.org/10.1007/BF00285901
Konarev A. The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. Theor Appl Genet. 1981 Mar;59(2):117-21. doi: 10.1007/BF00285901. PMID: 24276390.
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Two-step one-dimensional SDS-PAGE analysis of LMW subunits of glutelin : 1. Variation and genetic control of the subunits in hexaploid wheats.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Gupta RB, Shepherd KW.
PMID: 24220812
Theor Appl Genet. 1990 Jul;80(1):65-74. doi: 10.1007/BF00224017.

A collection of 222 hexaploid wheat cultivars (including the 207 cultivars studied by Gupta and Shepherd in 1988) from 32 countries was analyzed for variation in the banding patterns of LMW subunits of glutenin using a modified two-step 1-D...

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Gupta RB, Shepherd KW. Two-step one-dimensional SDS-PAGE analysis of LMW subunits of glutelin : 1. Variation and genetic control of the subunits in hexaploid wheats. Theor Appl Genet. 1990;80(1):65-74doi: 10.1007/BF00224017.
Gupta, R. B., & Shepherd, K. W. (1990). Two-step one-dimensional SDS-PAGE analysis of LMW subunits of glutelin : 1. Variation and genetic control of the subunits in hexaploid wheats. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 80(1), 65-74. https://doi.org/10.1007/BF00224017
Gupta, R B, and Shepherd, K W. "Two-step one-dimensional SDS-PAGE analysis of LMW subunits of glutelin : 1. Variation and genetic control of the subunits in hexaploid wheats." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 80,1 (1990): 65-74. doi: https://doi.org/10.1007/BF00224017
Gupta RB, Shepherd KW. Two-step one-dimensional SDS-PAGE analysis of LMW subunits of glutelin : 1. Variation and genetic control of the subunits in hexaploid wheats. Theor Appl Genet. 1990 Jul;80(1):65-74. doi: 10.1007/BF00224017. PMID: 24220812.
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Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris).

Planta

Pusztai A, Duncan I.
PMID: 24493138
Planta. 1971 Dec;96(4):317-25. doi: 10.1007/BF00386946.

Hydrolytic activity towards synthetic substrates and denatured proteins was measured in the extracts of the seeds of kidney bean at various stages of germination up to 16 days.Of the peptide hydrolases, chymotrypsin-type activity was stable for the first 7...

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Pusztai A, Duncan I. Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta. 1971;96(4):317-25doi: 10.1007/BF00386946.
Pusztai, A., & Duncan, I. (1971). Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta, 96(4), 317-25. https://doi.org/10.1007/BF00386946
Pusztai, A, and Duncan, I. "Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris)." Planta vol. 96,4 (1971): 317-25. doi: https://doi.org/10.1007/BF00386946
Pusztai A, Duncan I. Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta. 1971 Dec;96(4):317-25. doi: 10.1007/BF00386946. PMID: 24493138.
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Spectroscopic study on the interaction of pristine C60 and serum albumins in solution.

Nanoscale research letters

Liu S, Sui Y, Guo K, Yin Z, Gao X.
PMID: 22856352
Nanoscale Res Lett. 2012 Aug 02;7(1):433. doi: 10.1186/1556-276X-7-433.

The interaction of nanomaterials with biological macromolecules is an important foundation of the design and the biological safety assessments of nanomaterials. This work aims to investigate the interaction between pristine C60 and serum albumins (human serum albumin and bovine...

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Liu S, Sui Y, Guo K, et al. Spectroscopic study on the interaction of pristine C60 and serum albumins in solution. Nanoscale Res Lett. 2012;7(1):433doi: 10.1186/1556-276X-7-433.
Liu, S., Sui, Y., Guo, K., Yin, Z., & Gao, X. (2012). Spectroscopic study on the interaction of pristine C60 and serum albumins in solution. Nanoscale research letters, 7(1), 433. https://doi.org/10.1186/1556-276X-7-433
Liu, Shufang, et al. "Spectroscopic study on the interaction of pristine C60 and serum albumins in solution." Nanoscale research letters vol. 7,1 (2012): 433. doi: https://doi.org/10.1186/1556-276X-7-433
Liu S, Sui Y, Guo K, Yin Z, Gao X. Spectroscopic study on the interaction of pristine C60 and serum albumins in solution. Nanoscale Res Lett. 2012 Aug 02;7(1):433. doi: 10.1186/1556-276X-7-433. PMID: 22856352; PMCID: PMC3562194.
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Polymorphism of blood serum post-albumins in Lowland Black-and-White cattle of North-Western Poland.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Kawecki AM, Przytulski T.
PMID: 24419733
Theor Appl Genet. 1975 Jan;46(2):117-20. doi: 10.1007/BF00281650.

The authors showed polymorphism of the blood serum post-albumins in a population of Lowland Black-and-White cattle. Having tested 1001 samples of blood serum they found three Poa phenotypes, Poa FF, Poa SS and Poa FS, which were controlled by...

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Kawecki AM, Przytulski T. Polymorphism of blood serum post-albumins in Lowland Black-and-White cattle of North-Western Poland. Theor Appl Genet. 1975;46(2):117-20doi: 10.1007/BF00281650.
Kawecki, A. M., & Przytulski, T. (1975). Polymorphism of blood serum post-albumins in Lowland Black-and-White cattle of North-Western Poland. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 46(2), 117-20. https://doi.org/10.1007/BF00281650
Kawecki, A M, and Przytulski, T. "Polymorphism of blood serum post-albumins in Lowland Black-and-White cattle of North-Western Poland." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 46,2 (1975): 117-20. doi: https://doi.org/10.1007/BF00281650
Kawecki AM, Przytulski T. Polymorphism of blood serum post-albumins in Lowland Black-and-White cattle of North-Western Poland. Theor Appl Genet. 1975 Jan;46(2):117-20. doi: 10.1007/BF00281650. PMID: 24419733.
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Showing 13 to 24 of 218 entries