Synthesis of Hydroxyapatite in Microemulsion and its Adsorption Properties for Human Serum Albumin

2009 ◽  
Vol 79-82 ◽  
pp. 51-54
Author(s):  
Xian Peng Zheng ◽  
Yan Liu ◽  
Yan Ming Yang ◽  
Dong Wei ◽  
Yuan Yuan Xu ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Adsorption Capacity ◽  
Serum Protein ◽  
Ph Value ◽  
Energy Dispersive Spectrometer ◽  
High Surface ◽  
Size Analysis ◽  
Human Serum Protein

Hydroxyapatite (HAP) was synthesized in Triton X-100 microemulsion and was characterized by scanning electron microscopy (SEM), energy dispersive spectrometer (EDS). Particle size analysis results showed that the particles has nanometer size, high surface area and loose structure. The prepared HAP had high adsorption capacity to human serum protein and the adsorption of human serum protein on the surface of HAP was confirmed by SEM. The factors which influenced the adsorption capacity such as the acidity, reaction time and the concentration of adsorbent were investigated in detail and the adsorption isothermal was also obtained. The adsorption capacity reduced while the pH value increased, and the adsorption reached equilibrium when shaking time was up to 40 min. The adsorption isotherm could be fitted by the pseudo-Langmuir type. The adsorption of human serum albumin on HAP was investigated, and the influences of adsorption on the conformation of human serum albumin were studied by infrared and ultraviolet spectroscopy. It can be seen from the FT-IR spectra that the intensity of flex vibration of C=O, N-C bonds all weakened. The calculation results of ultraviolet spectrum indicated that the quantity of α spiral structure reduced from 44% to 17.12%.

Three turbidimetric methods for determining total protein compared.

1985 ◽  
Vol 31 (8) ◽  
pp. 1377-1380 ◽  
Author(s):  
H H Nishi ◽  
R J Elin
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Protein Concentration ◽  
Total Serum Protein ◽  
Total Serum ◽  
Benzethonium Chloride ◽  
Human Serum Protein ◽  
Biuret Method

Abstract We used human serum protein fractions to evaluate the sensitivity and bias of three turbidimetric methods for determining concentrations of proteins. Each fraction (Cohn Fractions II, III, IV, and V) was assigned a protein concentration value that was determined by the biuret method, which we calibrated with purified monomer of human serum albumin. All three turbidimetric methods (those involving sulfosalicylic acid/sodium sulfate, trichloroacetic acid, and alkaline benzethonium chloride) gave acceptable results for Fraction V with crystallized human serum albumin as the reference material, but there was bias by each of the three methods for the three globulin fractions. The method involving alkaline benzethonium chloride with measurement at 450 nm had the best sensitivity within the range of linearity and the most consistent bias among the three globulin fractions. These results define the dilemma for valid calibration of these methods for total serum protein in cerebrospinal fluid and urine.

THE ETIOLOGY OF HYPOPROTEINEMIA IN A PATIENT WITH CONGENITAL CHYLOUS ASCITES

PEDIATRICS ◽  
1962 ◽  
Vol 30 (5) ◽  
pp. 696-706
Author(s):  
Fred S. Rosen ◽  
David H. Smith ◽  
Ralph Earle ◽  
Charles A. Janeway ◽  
David Gitlin
Keyword(s):  
Gastrointestinal Tract ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Chylous Ascites ◽  
Lower Extremities ◽  
Characteristic Finding

An infant with congenital chylous ascites and Milroy's disease, as well as two patients with Milroy's disease of the lower extremities, have been studied with regard to the turnover of I131-labeled human serum albumin. The children with Milroy's diease had a normal turnover of radioiodinted albumin, whereas the child with congenital chylous ascites had a markedly increased turnover due to loss of serum protein into the gastrointestinal tract. The hypoproteinemia which is a characteristic finding in congenital chylous ascites may be due to such gastrointestinal loss of protein in serum.

Glycylglycylglycine as a Synthetic Standard for Serum Protein Determination

1974 ◽  
Vol 20 (1) ◽  
pp. 70-73
Author(s):  
Bernard Klein
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Molar Absorptivity ◽  
Protein Determination ◽  
Synthetic Standard ◽  
Mean Differences

Abstract Glycylglycylglycine was investigated as a reference standard for use in serum protein measurement by the biuret reaction. The tripeptide-biuret solution has a molar absorptivity of 96 at 565 nm, and absorbances at both 550 nm and 565 nm are proportional to concentration. By a manual reference procedure, the 550-nm absorbance of 1.0 g of tripeptide was equivalent to that given by 1.72 ± 0.03 g of human serum albumin or 1.43 ± 0.03 g of bovine serum albumin. By the Technicon N14b automated procedure, the absorbance of 1.0 g of tripeptide at 550 nm was equivalent to that of 1.81 ± 0.02 g of human serum albumin or 1.89 ± 0.03 g of bovine serum albumin. Results for serum protein analyses over the range 4.0 to 9.0 g/dl, when tripeptide or serum albumin was used to prepare calibration curves, showed mean differences of 0.15 g/dl in the manual mode and 0.08 g/dl in the automated mode.

scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

Standards for Total Serum Protein Assays— A Collaborative Study

1975 ◽  
Vol 21 (8) ◽  
pp. 1159-1166 ◽  
Author(s):  
Basil T Doumas
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Total Serum Protein ◽  
Total Serum ◽  
Final Reaction ◽  
Protein Assays

Abstract We have studied the standardization of total serum protein assay with the biuret reaction. Standard solutions were prepared from lyophilized preparations of human serum albumin and bovine serum albumin, with corrections made for volatile material and ash contents. These solutions and a solution of crystalline albumin standard were analyzed with a new stable biuret reagent, to establish absorptivity values (values for the absorbance of a 1 g/liter final reaction mixture). The mean values obtained were 0.302, 0.292, and 0.290 for human serum albumin, bovine serum albumin, and the crystalline albumin, respectively. We believe that the established absorptivity value will improve the accuracy of serum protein determinations. We studied the linearity of the relation between color produced and protein concentration, with use of the solutions described above and a serum pool. The color adheres to Beer's law up to the highest concentration tested: 3 g/liter for HSA and BSA, and 2.8 g/liter for serum in the final reaction mixture. The new biuret reagent has been stable for one year at room temperature. We recommend the use of bovine serum albumin as a primary standard for serum protein assays. It is inexpensive, easily available, and exhibits the best linearity in the biuret reaction.

scholarly journals FABRICATION AND EVALUATION OF HUMAN SERUM ALBUMIN (HSA) NANOPARTICLES FOR DRUG DELIVERY APPLICATION

2009 ◽  
Vol 08 (03) ◽  
pp. 319-322 ◽  
Author(s):  
R. MEHRAVAR ◽  
M. JAHANSHAHI ◽  
N. SAGHATOLESLAMI
Keyword(s):  
Drug Delivery ◽  
Particle Size ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ph Value ◽  
Drug Carrier ◽  
Particle Size Analyzer ◽  
Carrier Systems

Human Serum Albumin (HSA) nanoparticles represent promising drug carrier systems. Particle size is a crucial parameter in particular for the in vivo behavior of nanoparticles after intravenous injection. The object of present study was to characterize the desolvation process of HSA for preparation of nanoparticles. Two process parameters were examined to achieve a suitable size of nanoparticles such as the pH value and the amount of glutaraldehyde concentration (%). The smallest size of nanoparticles achieved was 91 nm and the largest size was 388 nm which is suitable for drug delivery. The pH value of the HSA solution prior to the desolvation procedure was identified as the major factor determining particle size and the amount of crosslinker showed that it has less effect on produced nanoparticle size. The nanoparticle sample was purified by five cycles' centrifugation (20 000× g, 8 min) and redispersion of the pellet to the original volume in 10 mM NaCl at pH values of 7.5–9, respectively, and then analyzed by particle size analyzer (PCS).

scholarly journals Effects of Urinary Macromolecules on Hydroxyapatite Crystal Formation

2001 ◽  
Vol 12 (10) ◽  
pp. 2108-2116
Author(s):  
ANN M. BESHENSKY ◽  
JEFFREY A. WESSON ◽  
ELAINE M. WORCESTER ◽  
ELENA J. SOROKINA ◽  
CARL J. SNYDER ◽  
...  
Keyword(s):  
Crystal Growth ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chondroitin Sulfate ◽  
Crystal Surface ◽  
Size Analysis ◽  
Crystal Formation ◽  
Secondary Nucleation ◽  
Urinary Macromolecules

Abstract. Particle size analysis was combined with titration data obtained in constant-composition, hydroxyapatite (HA)-seeded, crystal growth assays. With addition of large amounts of HA (250 μg), titration rates were linear, new crystal formation was minimal, and aggregation effects could be detected. With addition of small amounts of HA (62.5 μg), nucleation of new HA was observed. The effects of urinary macromolecules, i.e., osteopontin (OPN), recombinant glutathione-S-transferase-OPN (G-OPN), Tamm-Horsfall protein, chondroitin sulfate, human serum albumin, mixed urinary macromolecules from a stone-former (SFU1), mixed urinary macromolecules from a normal individual (NU1), and polyaspartic acid (PA), were examined in this system. Crystal growth inhibition, as measured by the slope of linear titration curves in this system, was observed with PA, G-OPN, OPN, SFU1, and NU1. All of the macromolecules tested inhibited aggregation, including Tamm-Horsfall protein, which did not inhibit growth. As reflected by the ratio of the final number of particles to the initial number in the 62.5-μg seed addition, the macromolecules that were most effective in inhibiting growth, i.e., OPN, G-OPN, PA, SFU1, and NU1, actually increased secondary nucleation. Recombinant G-OPN demonstrated less inhibitory activity than did OPN isolated from cell culture. Chondroitin sulfate and human serum albumin exhibited no significant effects on the various components of HA crystallization under these conditions. SFU1 and NU1 slowed growth and increased secondary nucleation to similar degrees, and neither exhibited any measurable effect on aggregation. Therefore, crystal surface sites that participate in nucleation, growth, and aggregation processes are affected independently by macromolecules, presumably because of differences in their structural features. These results illustrate the utility of combining these techniques to provide a much greater understanding of crystallization behavior than that possible with either analysis alone.

II. Lokalisation der Placenta mit 113Inm- Human-Serum-Albumin

1969 ◽  
Vol 08 (01) ◽  
pp. 15-21 ◽  
Author(s):  
K. E. Scheer ◽  
J. Heep ◽  
W. Maier-Borst ◽  
W. J. Lorenz ◽  
H. Sinn ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Vena Cava ◽  
Placenta Praevia ◽  
Wird Eine

ZusammenfassungNach tierexperimentellen Voruntersuchungen wurde die Placentographie mit trägerfreiem 113Inm -HSA als klinische Methode eingeführt. Vor Amniocentesen und bei Verdacht auf Placenta praevia werden Placentographien geschrieben. Den Schwangeren wird eine Aktivität von 500 μCi in die Cubitalvene injiziert. Die der Aktivität entsprechende Indiummenge ist kleiner als 0,1 ng. Die fetale Strahlenbelastung liegt unter lOmrad. Bei Anwendung von 113Inm-HSA entfällt eine Blockade der mütterlichen und fetalen Schilddrüsen. Die genaue Abgrenzung einer Placenta praevia wird nicht durch eine Blasenaktivität beeinträchtigt.Es wurden bisher 19 Placentalokalisationen durchgeführt. In allen Fällen konnte der Placentasitz eindeutig festgestellt werden. Bedingt durch die lange Liegezeit beim Aufnehmen eines Szintigramms kam es in zwei Fällen zu einem Vena-Cava-Kompressions-Syndrom. Zur Verhinderung dieser klinischen Zwischenfälle werden inzwischen Placentographien mit der Anger-Kamera aufgenommen. Mit Hilfe des divergierenden Kollimators konnte der gesamte Abdominalbereich erfaßt werden. Die Aufnahmezeit konnte auf 7 — 10 Minuten verkürzt werden. Die intravenöse injizierte Aktivität betrug bei dieser Methode ebenfalls 500 μCi. Der diagnostische Aussagewert der Kamerabilder ist szintigraphischen Aufnahmen gleichwertig.

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