Inhibition of calcium oxalate crystallization by commercial human serum albumin and human urinary albumin isolated from two different race groups: evidence for possible molecular differences

2006 ◽  
Vol 34 (6) ◽  
pp. 373-380 ◽  
Author(s):  
Allen L. Rodgers ◽  
Priscilla D. Mensah ◽  
Sylva L. Schwager ◽  
Edward D. Sturrock
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Calcium Oxalate ◽  
Human Serum ◽  
Urinary Albumin ◽  
Calcium Oxalate Crystallization

Exploring the Molecular Level Interaction of Human Serum Albumin with Calcium Oxalate Monohydrate Crystals

2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao
Keyword(s):  
Amino Acids ◽  
Crystal Growth ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Calcium Oxalate ◽  
Human Serum ◽  
Stone Formation ◽  
Calcium Oxalate Monohydrate ◽  
Calcium Oxalate Crystallization ◽  
In Silico Docking

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.

Laser immunonephelometry for routine quantification of urinary albumin excretion.

1987 ◽  
Vol 33 (2) ◽  
pp. 209-213 ◽  
Author(s):  
M Marre ◽  
J P Claudel ◽  
P Ciret ◽  
N Luis ◽  
L Suarez ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Room Temperature ◽  
Normal Values ◽  
Urinary Albumin Excretion ◽  
Urinary Albumin ◽  
Albumin Excretion ◽  
Large Numbers ◽  
Time Of Collection

Abstract We describe a laser-immunonephelometric method for quantifying urinary albumin excretion (UAE) in large numbers of samples. For a 150-microL sample incubated at room temperature for 45 min with 40 microL of antiserum specific for human serum albumin, the assay range for albumin was 0.34 to 43.0 mg/L. For samples analyzed undiluted and diluted 10-fold, the range of measurable albumin was from 0.34 to 430.0 mg/L. With an automated version of this method, one can assay 240 samples per hour. Intra- and interassay CVs were less than 6% and 9%, respectively. Measurements by this method (y) correlated well with those obtained by a RIA method (x): y = 1.00x + 0.163 mg/L (n = 233; r = 0.996). The day-to-day CV for UAE was determined for three consecutive determinations done on each of 60 controls according to the time of collection and in 212 diabetics according to the amount of 24-h UAE. For controls, UAE was 8.0 +/- 8.1 mg/24 h (mean +/- SD), CV 44 +/- 23%. The CV was similar for diurnal (50 +/- 28%) and overnight (58 +/- 32%) collections from controls; and for diabetics with normal values for UAE: 35 +/- 32%, with slight albuminuria (25-300 mg/24 h):37 +/- 28%, or with macroalbuminuria (greater than 300 mg/24 h): 47 +/- 42%.

scholarly journals Preparation of highly purified monomeric human serum albumin as secondary reference material for standardization of urinary albumin immunoassays

2012 ◽  
Vol 413 (1-2) ◽  
pp. 175-181 ◽  
Author(s):  
Yoshihisa Itoh ◽  
Kiyoshi Ichihara ◽  
Kouji Kishi ◽  
Shigemi Hosogaya ◽  
Toshiyuki Yamada
Keyword(s):  
Reference Material ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Urinary Albumin

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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