Bovine serum albumin (BSA or Fraction V) is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname Fraction V refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean.The standard nomenclature to represent the isoelectric point is pH(I). However, pI is also used. For brevity, this article uses pI. The net charge on the molecule is affected by pH of its surrounding environment and can become more positively. Bovine serum albumin (BSA, isoelectric point = 5.4) was used as a model protein and DEAE Sepharose FF as an ion exchanger. Finite batch adsorption experiments and isocratic elution chromatography were performed for the determination of the model parameters (i.e., characteristic charge, equilibrium constant, and steric factor). The results showed that pH had significant effects on the. Bsa Isoelectric Point. Source(s): https://shrinks.im/batTs. 0 0. ordaz. Lv 4. 4 years ago. Isoelectric Point Of Bsa. Source(s): https://shrinke.im/a0CTQ. 0 0. Alan F. Lv 6. 9 years ago. Draw a graph is the obvious answer, which you have, I assume pH against distance. From the graph somewhere between pH 5 and 6, and between pH 6 and 7 you will find the distance is zero . Source(s): School. 0 0.
According to the literature [31, 32], the isoelectric point (pI) of BSA is in the range of 4.7-5. Other scientists cal-culated that the above point of BSA is equal to 5.56 . BSA is classiﬁed as 'soft' protein, i.e. of low internal sta-bility . It was found that at neutral pH, a-helix accounts for 54 % and b-sheet represents about 16-18 % of the BSA chain . Then it is of. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO 2 complex with a value of ca. 3 ± 1 × 10 11 molecules cm −2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below Bovine serum albumin (BSA)-capped gold NPs (c. 12 nm) in agarose gel membrane (Au NPs/BSA/AGM) has been developed for removing Hg 2+ or Pb 2+ in saline solution [124-126]. On the other hand, Wei et al.  prepared gold nanoparticle/bacterial cellulose (AuNP/BC) nanocomposites by citrate-mediated in situ reduction of Au 3+ in the presence of a BC hydrogel Theoretical titration curves of BSA protein in a wide range of pH values and for pH values close to the point of zero charge (inset); in the presence of di ff erent concentrations (0.1 to 0.5 M.
The isoelectric points of ovalbumin at different concentrations in buffers at 0 ionic strength plotted against the concentration of the protein. 0 represents values from mobility measurements; mini- mal pH change. strength of buffer for each protein concentration are plotted against the percentage concentrations of albumin; these three points fall on a straight line which intercepts the axis. isoelectric point in water at 25 °C: 4.7; Extinction coefficient of 43,824 M −1 cm −1 at 279 nm BSA has been widely used as a template to synthesize nanostructures. BSA is also the main constituent of fetal bovine serum, a common cell culture medium. See also. Acceptable daily intake ; Protein allergy; Human serum albumin; Serum albumin; References. Further reading. Hirayama K, Akashi. Isoelectric point of glycated BSA. The change in the isoelectric point of BSA after glycation was analyzed by isoelectric focusing in polyacrylamide gels using a FastSystem (Pharmacia, Uppsala, Sweden). The bands were dyed with silver nitrate, and the isoelectric point was evaluated using the analytical unit of FastSystem employing a broad.
Isoelectric point (pI): The pH at which the net charge on the protein is zero. For a protein with many basic amino acids, the pI will be high, while for an acidic protein the pI will be lower. Isoelectric focusing is a type of zone electrophoresis, and it is usually performed in a gel, that takes advantage of the fact that a molecule's charge changes with the pH of its surroundings. A protein. BSA protein (lyophilized powder ≥96%, mol weight ~66 kDa, Sigma-Aldrich) was prepared by dissolving 1 mg/ml in 0.01 M NaCl solution adjusted to three different pH values (4.5, 5.0, and 5.5). These pH values were chosen, because they are close to the isoelectric point, or zero charge point, of the BSA protein [45, 46]. It should be made clear. BSA is a protein composed of many, many amino acids, so there would be way too many Ka's to be able to figure out the isoelectric point in this way. What would be the effect on migration distances in exp 2 if higher voltage was used? they would increase, because the strength of the electric field would increase based on its equation E=V/d . Why does molecular weight influence electrophoretic. Isoelectric point 5.7 - 7.6 (6.6 +/- 0.9 Davalos-Patoja et al. 2000) The most hydrophobic moiety of IgY molecule is the Fc fragment (Schade et al. 2005) Extinction coefficient (i.e. absorbance of a 10 mg/ml solution at 280 nm) are: in 0.3 M KCl = 13.18; in 0.1 M NaOH = 14.4; in 5 M guanidine = 12.7 (Leslie and Clem 1969) Weight of IgY (or other protein) to molar quantity can be converted here. Enzyme Immunoassays From Concept to Product Development. Authors (view affiliations) S. S. Deshpand
How do amino acids look like at the isoelectric point? 0. How do I calculate the ensemble-average net charge of an amino acid at given pH? 6. How can I properly calculate the isoelectric point (pI) of amino acids? 1. Why are Tyrosine and Tryptophan considered hydrophobic? 1. Why are amino acids least soluble at isoelectric point? Hot Network Questions Is there an easy way to give temporary. How can I determine the isoelectric point of BSA? What I have is a graph of the average distance BSA traveled at various pHs, and I need some way to deduce the pH at which it (theoretically) wouldn't have moved at all. Can anyone offer some insight? pH Average Distance (cm) 4 -0.2. 4.5 -0.9. 5 -1.3. 6 3.9. 7 -1.5. Responder Guardar. 4 respuestas. Relevancia. blackbeauty14. Lv 5. hace 9 años. The isoelectric point (pI) of a peptide is defined as the pH at which the peptide has a net charge of zero. At pH values below the pI, peptides carry a net positive charge; Above the pI, they carry a net negative charge. pI-values of peptides can be utilized as a basis for separation in solution. If a voltage is applied to a complex peptide mixture in a pH gradient, the peptide will migrate to. The isoelectric point (pI) of IgG antibodies ranges between 6.8 and 8.5. The isoelectric point predicts where a protein has a net overall charge of zero. By adjusting the pH of the buffer above or Thebelow the pI the overall charge of the protein can be made negative or positive. Non-specific experiments were conducted using three commonly used buffers: MES buffer pH 6.0, 1x phosphate buffered.
等电点是一个分子表面不带电荷时的pH值。是针对带电荷的物质而言，不只限于两性电解质如氨基酸和蛋白质。当然，蛋白质是两性电解质，其等电点和它所含的酸性氨基酸和碱性氨基酸的数量比例有关。各种蛋白质因氨基酸残基组成不同，等电点也不一样。当溶液在某一特定pH值的条件下，蛋白质. On the other hand, BSA adsorbed homogeneously onto the OTS and FOETS phases at the isoelectric point of BSA (pH 4.7). These results indicate that the preferential adsorption of BSA onto the FOETS phase in the mixed (OTS/FOETS) monolayer system is due to: (1) the minimization of the interfacial free energy between a monolayer surface and an aqueous solution; and (2) the electrostatic repulsion. The permeability of the protein deposits decreased with increasing solution ionic strength at pH both above and below the protein isoelectric point but was relatively independent of ionic strength at the isoelectric point. The permeability of the BSA deposits at neutral pH was markedly smaller when measured with solutions of divalent cations than with solutions of monovalent cations but was. AURION BSA-c™ concentrated solution contains acetylated bovine serum albumin as the functional constituent. By acetylation of amines on basic amino acids these groups are no longer as easily protonated and the isoelectric point of such molecules is lowered and hydrophobicity is increased. BSA-c™ is a 10% solution of acetylated BSA at. Bovine serum albumin (BSA) was modifed by covalent attachment of chlorogenic acid using different concentrations at pH 9. The derivatization was accompanied by a reduction of lysine, cysteine and tryptophan residues. The isoelectric points were shifted to lower pH values and formation of high molecular weight fractions was noted. The structural changes were studied using circular dichroism.
The effects of heat treatment of calcium hydroxyapatite (Hap) on the protein adsorption behavior were examined using typical proteins of bovine serum albumin (BSA: isoelectric point (iep) = 4.7, molecular mass (Ms) = 67,200 Da, acidic protein), myoglobin (MGB: iep = 7.0, Ms = 17,800 Da, neutral prot Principles of life space in child and youth care Actually Practice Exam 9 2017, questions and answers Visual arts and design semester 1 Lab 3 Electrophoresis of amino acids Report Lab 6 Isolation & Identification of Egg White Proteins report Lab 1 Spectrophotometry Repor
isoelectric points in the bulk: B4.8 for BSA,53 7.0 for HbA,54 7.4 for Mb,55,56 and 11.3 for Lz.57 We show that HD-VSFG is sensitive enough to detect the decrease by one pH unit of the isoelectric point of human hemoglobin at the air/water interface. Experimental Proteins Human adult hemoglobin was obtained from fresh blood drawn into tubes containing ethyldiaminetetraacetate by venipuncture. Experiment #2: The Determination of the Isoelectric Point of the Protein Bovine Serum Albumin Name: Lab Partner Name(s): Date: TA Name: Course Listing: CHEM Lab Room - I pledge that I have not used someone else's old or current lab report when writing this lab report. I pledge that I did not collaborate with any other students and that the report I submitted here contains my own. isoelektrischer Punkt, Kurzzeichen pI oder IEP, der pH-Wert, bei dem die Gesamtladung (elektrische Ladung) eines zwitterionisch (Zwitterionen) aufgebauten Moleküls (z.B. einer Aminosäure, eines Peptids, Proteins oder Nucleotids) neutral ist, d.h. gleichviel positive wie negative Ladungen vorliegen. Der isoelektrische Punkt ist eine für jedes einzelne zwitterionisch aufgebaute Molekül. values above the isoelectric point of the proteins under which the polyelectrolytes and the pro teins are like-charged. All data published so far demonstrate that this type of adsorption becomes weaker with increasing ionic strength. A much stronger interaction is found if the polyelectrolyte chains are grafted onto solid surfaces to form polyelectrolyte brushes. Here it has been ·shown that. BSA is a protein composed of 583 aminoacid residues, has molar mass of 66430g/gmol, is very soluble in water (it can be precipitated in high concentrations of a neutral salt, such as ammonium sulphate), has isoelectric point in the pH range of 4.60-5.70, and presents spheroidal shape, characteristic sizes of 4nm × 4nm × 14nm and Stoke radius of 3.48nm [38-40]
Provided is a method for measuring isoelectric point which can be more easily and quickly carried out than conventional methods and by which highly reliable and objective data can be obtained. The method for measuring isoelectric point according to the present invention, whereby the isoelectric point of a substance (test substance) with unknown isoelectric point is measured by an. Isoelectric Point (IEP) Determination (BSA) were diluted 1:100 with DI water. This BSA solution was brought to pH 8 with 0.1 M KOH and titrated with 0.01 M HCl to a final pH of 3.75. Three zeta potential measurements were taken at each pH value and the average was calculated. FOR MORE INFORMATION Please call your Regional Customer Service Center today to learn what Entegris can do for you. If the isoelectric pH of a particle exists between the two electrodes, the particle will migrate toward its isoelectric point, and effectively stop when it reaches its isoelectric pH. Shrinking the apparatus to microfluidic dimensions should allows fractionation of particles with a small voltage perpendicular to the flow in an H-filter. The proteins, bacteria, or other charged particles would. Fingerprint Dive into the research topics of 'Investigation of bovine serum albumin (BSA) attachment onto self-assembled monolayers (SAMs) using combinatorial quartz crystal microbalance with dissipation (QCM-D) and spectroscopic ellipsometry (SE)'. Together they form a unique fingerprint. Sort by Weigh The molecular weight of ovalbumin is 171,391.45 Da, and its isoelectric point (pI) is 5.19 (7). The major significance of ovalbumin does not reside in its biological function as a molecule. Ovalbumin provides a major interest for study because its structure provides a model for the structure of the inhibitory serpins. To understand this, a background to the structure and function of serpins is.
You searched for: Subject isoelectric point Remove constraint Subject: isoelectric point Start Over. Toggle facets Limit your search Text Availability. Citation in PubAg 2,739; Full Text 184; Journal. Fish & shellfish immunology 120; Food hydrocolloids 110; Colloids and surfaces 99; Journal of agricultural and food chemistry 91; Langmuir 71; more Journal » Publication Year. 2020 99; 2019. The high isoelectric point of this molecule (pI = 10.8) at pH 7.0 and its small molecular dimensions (2.5 by 2.5 by 3.7 nm) allow it to fit into very small spaces on bacterial surfaces (primary source). Entered by: Uri M: ID: 108066: Related BioNumbers. Membrane conductance. Unspecified ID: 110760 τ=(Cm/Gm)=(membrane capacitance)/(membrane conductance) Unspecified ID: 110761 Specific membrane.
Bovine serum albumin (BSA, MW 66 kDa, isoelectric point (pI) 4.7) and lysozyme (LYZ, MW 14.3 kDa, pI 11.4) from chicken egg white were bought from Sigma Aldrich. Synthesis of functionalized castor oil (ICO). A solvent-free reaction was used to functionalize castor oil with a silica precursor (IPTES) as coupling agent to obtain castor oil with cross- linkable functions. The reaction was. isoelectric point (pI) of 8.5  and a size of 26 kDa , is buffered at pH 4.5 after reconstitution. At this pH, the protein has a strong positive charge and is considered to be largely soluble. However, Schwartz et al. demonstrated by size exclusion chromatography that the protein is partially aggregated in this buffer . They also found that BMP-2 retains its full integrity in the. Isoelectric point: ~5.0 Michaelis constant (Phosphate buffer, 0.5 mol/l, pH 7.5; +25°C): Cholesterol: 1 x 10-4 mol/L Inhibitors: Hg 2+, ZnCl 2, SDS Activators: Non ionic detergents pH optimum: 5.5-8.0 (see figure) Temperature dependence: See figure pH stability: 5.0-10.0 (see figure) Thermal stability: Up to +55°C (see figure) Storage and Stability: No decrease in activity over 6 weeks at.
After equilibrium sorption was reached at pH 7.0, desorption of bovine serum albumin occurred when pH was lowered to 2.0, which is below the isoelectric point of bovine serum albumin. Our data provide further evidence that combinatorial quartz crystal microbalance with dissipation and spectroscopic ellipsometry is a sensitive analytical tool to evaluate attachment and detachment of adsorbed. The sieving coefficients and hydraulic permeability were both maximum at the BSA isoelectric point. The sieving coefficients decreased with increasing ionic strength at pH above and below the isoelectric point and were also a function of the ionic composition (Na + vs Ca 2+) of the solvent. These results, in combination with independent measurements of the hydraulic permeability, were used to. . The majority of conventional methods for the determination of the isoelectric point of a molecule rely on the use of spatial gradients in pH, although significant practical challenges are associated with such techniques, notably the diﬃculty in generating a stable and well. By isoelectric focusing in a column with a sucrose density gradient of native BSA monomer Rosseneu-Motreff et al.9) demonstrated three fractions with isoelectric points of 4.89, 5.22, and 5.59, and it was ascertained that bovine albumin complexed with fatty acids was focused near pH 4.9. On the othe
Solution for The speed with which the protein bovine serum albumin (BSA) moves through water under the influence of an electric field was monitored at severa Asymmetrical isoelectric point (pI) was a characteristic of M802. The monomer or homodimer of monovalent unit's pI was about 7.8, and the monomer or homodimer of single chain unit's pI is about 8.9, while M802's pI was about 8.5 (Fig. 1d). The unique properties of M802 were used for purification of this BsAb using ion-exchange. In proteins the isoelectric point (pI) is defined as the pH at which a protein has no net charge. When the pH > pI, a protein has a net negative charge and when the pH < pI, a protein has a net positive charge. The pI varies from protein to protein. This is the reason ion exchange is useful for separating proteins. If a buffer containing more than one protein is used with an anion exchange. Native BSA ** monomers gave, in the electrofocusing pattern, three peaks with pI values 4.84, 5.15, and 5.39. After exposure to alkali, apparent shifts in the isoelectric point of some of the peaks and the appearance of new peaks with pI values 5.48, 5. 52, 5.70, 5.85, and 5.91 were observed You can fix this problem by preparing a buffer with a pH within the isoelectric point range (predicted neutral overall charge) of your protein. 2) Use Additives - Protein Blocker If you are using a protein as your analyte, you can always try using bovine serum albumin (BSA) in your buffer and samples to help prevent non-specific binding. BSA is a globular protein with hydrophilic and.
Indeed, when the pH buffer is equal to the pI (isoelectric point), the protein has no charge. Consequently, the protein is not able to bind to an ion exchange column (anion and cation). Adjusting the pH below or above the protein pI induces a positive charge when pH < pI and a negative charge when pH > pI (Fig.1). Fig.1: Protein charge is function of Buffer pH. When the protein has the. Protein samples were prepared by diluting bovine serum albumin (BSA) from Sigma Aldrich with DI water in 1:100 proportion. The BSA solution was mixed with 0.1M KOH to alter the pH to 8 and titrated using 0.1M HCl to achieve a final pH of 3.75. At each pH value, three zeta potential measurements were carried out, and the average value was obtained. Figure 4 shows the volume-weighted mean. In this research, bovine serum albumin (BSA) with a different isoelectric point value (4.7, 6.0 and 9.3) was synthesized and incorporated into a CS-SA based gene delivery system. CS-SA/DNA binary complexes and CS-SA/BSA/DNA ternary complexes were then prepared and characterized. The binding ability of the CS-SA vector with DNA was not affected by the incorporation of BSA. However, referring to.
Proteins are diverse in their composition and structure, and with some assays the proteins' differences in amino acid sequence, isoelectric point (pI), secondary structure, and side chains or prosthetic groups result in variation in the colorimetric response. This low protein-to-protein variation leads to higher accuracy in determining protein concentration for unknown protein samples At a pH above the isoelectric point, the negatively charged BSA molecules do adsorb onto the negatively charged silica surface, but change their sol-vation states. Indeed the residual NH content of BSA decreases from 20% to around 5% as the surface coverage increases on the negatively charged silica. This change in tertiary structure due to the contact of the protein with the repelling silica. Moreover, FO membrane fouling became much more significant at solution pH 4.7 (the BSA isoelectric point), where BSA molecules were neutrally charged and had no electrostatic repulsion among themselves. It was also demonstrated that the presence of alginate (a model polysaccharide) as co-foulant aggravated the BSA fouling of FO membrane, which could be attributed to the remarkable contribution. Start studying Experiment 2: Determination of the Isoelectric Point of the Protein Bovine Serum Albumin. Learn vocabulary, terms, and more with flashcards, games, and other study tools
Isoelectric Point pI 4.7-4.95 (1), 4.9-5.1 (2) (1) Miller & Gemeiner 1993 (2) Wal 1998: Amino Acid Sequence, mRNA, and cDNA. BSA : SWISS-PROT: P02769: GenBank: M73993, X58989, Y17769: PIR: ABBOS : Amino acids: 583 residues (1), 607 (precursor) mRNA: 2035 bp, 2061 bp, 1883 bp: cDNA (1) Brown 1975: Posttranslational Modifications Disulfide Bridges: 9 disulfide bonds (1) (1) Brown 1974. influence of pH and sodium chloride concentration on BSA rejection and permeate flux. Solutions with BSA concentration of 0.25 g/dm3 and NaCl concentration of 0, 5 and 25 mM were used at pH range of 4.0-8.0. The highest BSA transmission was ob-tained at pH of 4.9 corresponding to the isoelectric point of BSA. An addition o Separates proteins of various sizes, hydrophobicities, and isoelectric points Available in 3.5 μm particles for HPLC and 1.7 μm material for UPLC® and nano UPLC applications Maximizes recovery and minimizes protein carryover Tolerates extreme pH and temperature Quality-control tested with protein mixture Couples directly to ESI-MS for protein identification Protein Separation Technology. AU. Since BSA is much larger than DNA, such a high loading can only be explained multilayer adsorption (Dominguez-Medina et al., 2013). BSA has an isoelectric point of 4.7, and the adsorption was further promoted by lowering the pH below it, which can be attributed to the electrostatic attraction effect with negatively charged AuNPs isoelectric point, positively charged, and bind only to a cation exchanger. Proteins are eluted in the order of their net charge. 2. Less acidic pH: the blue protein is above its isoelectric point, negatively charged, and the other proteins are still positively charged. Blue protein binds to an anion exchanger and can be separated from the other proteins which wash through. Alternatively, red.
Isoelectric point 6.1-8.5 (7.3 +/-1.2) if monoclonal (polyclonal antibodies do not have a set isoelectric point as they are a pool of various classes). Isoelectric point 6.1-8.5 (7.3 +/-1.2), polyclonal antibodies do not have a set isoelectric point as they are a pool of various classes; Concentration in serum: 10-20 mg/ml; Glycosylation (by. Because this value is close to the isoelectric point of serum albumin. The surface structural change of BSA and diatomite clay was studied. For this, Fourier transform infrared spectroscopy (FTIR) spectroscopy values were compared before and after the experiment. The diatomite samples used as support material were characterized by FTIR, scanning electron microscopy, thermogravimetric analysis.
Company Telephone: Fax: Hours: Monday to Friday 8:30 - 17:30 PST (GMT-8) Location: 520 Mercury Driv Eigenschaften . Albumine haben eine Molare Masse von 66.248 Da und sind von elliptischer Gestalt. Sie bestehen aus 584 Aminosäuren, wovon viele schwefelhaltig sind.Sie sind wasserlöslich, ihre Bindungskapazität für Wasser beträgt ca. 18 ml/g. Der isoelektrische Punkt liegt bei 4,6. Albumine sind Ampholyte, d. h. im Gegensatz zu anderen Kolloiden oder Kristalloiden können sie sowohl. Proteins have characteristic salting out points, and these are used in protein separations in crude extracts. •The most effective region of salting out is at the isoelectric point of the protein because all proteins exhibit minimum solubility in solutions of constant ionic strength at their isoelectric points. 5 •The salt commonly used is ammonium sulfate because: •Its large solubility. The two proteins have significantly different isoelectric points, 11.35 for lysozyme and 5.4 for BSA. This difference in isoelectric point implies that the two particles would behave differently in an EK device. SPNPs were synthesized using two main proteins: lysozyme (SPNP-Lys-488) or BSA (SPNP-BSA-488). The particles were fully characterized . SPNP-Lys-488s had a size distribution and ζ p.
A Simple Method for Improving Protein Solubility and Long-Term Stability Alexander P. Golovanov,*,† Guillaume M. Hautbergue,‡ Stuart A. Wilson,‡ and Lu-Yun Lian*,† Contibution from the Department of Biomolecular Sciences, UniVersity of Manchester Institute o protein isoelectric point, using BSA as an example, and compares the data acquired with that obtained using other charge-measuring techniques. Experimental Figure 1: A: Zetasizer Nano ZSP; B: Cell entirely filled with blue dextran in 10 mM NaCl and cell filled with 10 mM NaCl loaded with 50 μl blue dextran to demonstrate the diffusion barrier technique. The electrophoretic mobility of 5.0 mg. Isoelectric Point: 6.97 (Theoretical) Extinction Coefficient: 13,940 cm-1 M-1 (Theoretical) E 1%,280 = 8.23 (Theoretical) Applications: Protein folding studies; Molecular weight marker; Standard for mass spectroscopy; ELIS
At equilibrium the chemical potential of BSA in solution equals that at each location in the brush, while the net force on the polyions (including osmotic, stretching, and excluded volume terms) is zero at each location. Protein adsorption is predicted above the isoelectric point and in agreement with experimental data− is a strong function of ionic strength and pH. Adsorption of protein in. point of BSA, ˘pH 5.9 At the isoelectric point, the water features nearly vanish. More importantly, these peaks carry a negative sign at high pH and a positive sign at low pH, indicating that orientation of the interfacial water molecules flips. Similar observations were made in previous VSFS studies of BSA as well as other proteins.8 When 8 M urea was introduced to the solution, a new peak. The result indicated that the adsorption capacity was very low when the pH of BSA solutions was above the isoelectric point of BSA. Original language: English: Pages (from-to) 350-355: Journal: Acta polymerica sinica = Gaofenzi xuebao: Volume: 2: Publication status: Published - 2006: Fingerprint; Bovine Serum Albumin. Adsorbents. Resins. Adsorption . Pore structure. Ion exchange. Cation. Competitive adsorption of albumin and monoclonal immuno upsilon globulin molecules on polystyrene surface
The composition of claim 1, wherein said at least one protein having a low isoelectric point is BSA. 4. The composition of claim 1, wherein said at least one protein having a low isoelectric point is selected from the group consisting of β-lactoglobulin, apomyoglobin, α-lactoalbumin, apotransferrin, α-acid glycoprotein, and β-casein. 5. The composition of claim 1, wherein said at least one. This pH value was the isoelectric point of BSA. At low [BSA] of 20 pM, protein molecules adsorbed as monomers. At intermediate [BSA] of 500 pM, protein molecules adsorbed as clusters of about five monomers on average. Both monomers and clusters had adsorption rate coefficients of the order 10−7 m s−1 and desorption rate coefficients of about 2 × 10−2 s−1. The respective steady-state. Transcapillary escape rate (TER) and initial distribution volume for (125)I-labeled bovine serum albumin (BSA, isoelectric point pH 4.6) and for (131)I-labeled charge modified BSA (cBSA, average isoelectric point, pH 7.1) was measured 3h after sepsis was induced by cecal ligation and incision (CLI) (n=11) and in control animals (n=12). The importance of charge for permeability in sepsis was.