Effective reduction of non-specific binding by bovine serum albumin modified quantum dot surface for cell targeted imaging

2014 ◽  
Author(s):  
Qian Wang ◽  
Min Zhang ◽  
Ling Wang ◽  
Yueqing Gu
Keyword(s):  
Bovine Serum Albumin ◽  
Quantum Dot ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Targeted Imaging ◽  
Effective Reduction

Effective Reduction of Nonspecific Binding by Surface Engineering of Quantum Dots with Bovine Serum Albumin for Cell-Targeted Imaging

Langmuir ◽  
2012 ◽  
Vol 28 (48) ◽  
pp. 16605-16613 ◽  
Author(s):  
Bingbo Zhang ◽  
Xiaohui Wang ◽  
Fengjun Liu ◽  
Yingsheng Cheng ◽  
Donglu Shi
Keyword(s):  
Quantum Dots ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Surface Engineering ◽  
Targeted Imaging ◽  
Nonspecific Binding ◽  
Effective Reduction

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin

2009 ◽  
Vol 407 (18) ◽  
pp. 5019-5023 ◽  
Author(s):  
Lingzi Zhao ◽  
Rutao Liu ◽  
Xingchen Zhao ◽  
Bingjun Yang ◽  
Canzhu Gao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Quantum Dot ◽  
Serum Albumin ◽  
Bovine Serum ◽  
New Strategy ◽  
Cdte Quantum Dot

scholarly journals Histochemical demonstration of estrogen and progesterone binding in endometriotic tissue and in uterine endometrium: A comparative study.

1985 ◽  
Vol 33 (2) ◽  
pp. 155-161 ◽  
Author(s):  
A Bergqvist ◽  
S Jeppsson ◽  
O Ljungberg
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Relative Proportion ◽  
Fluorescein Isothiocyanate ◽  
Histochemical Demonstration ◽  
Endometrial Tissue ◽  
Menstrual Phase ◽  
Uterine Endometrium

Estrogen and progesterone binding to endometriotic and endometrial tissue was studied histochemically using estradiol and progesterone fluorochrome derivatives (E2-bovine serum albumin-fluorescein isothiocyanate and progesterone-bovine serum albumin-tetramethylrhodamine isothiocyanate). Thirty endometriotic samples from 21 women were studied, together with endometrial specimens obtained simultaneously from 14 of the women. In 77% of the endometriotic samples binding of the estrogen conjugate was indicated by specific fluorescence in more than half of the epithelial cell population, and in 20% in less than half. The corresponding figures for the progesterone conjugate binding were 75 and 18%, respectively. Blocking studies indicated a reasonable degree of ligand specificity. In endometrial tissue the corresponding figures were 64 and 29%, respectively, for binding of the estrogen conjugate and 54 and 38%, respectively, for binding of the progesterone conjugate. In 7 of 13 cases where evaluable samples of both tissues had been obtained, the relative proportion of fluorescent cells, with either reagent, was similar in the two tissue types. Our results suggest that the cytoplasm of epithelial cells in endometriotic tissue and in uterine endometrium contains specific binding sites for both estrogen and progesterone. The binding pattern of the two conjugates in endometriotic tissue was unrelated to the menstrual phase.

scholarly journals The comparative specificity of three oestradiol-binding proteins. Rat α-foetoprotein, rat liver 17β-hydroxy steroid dehydrogenase and anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) antiserum

1975 ◽  
Vol 151 (3) ◽  
pp. 513-518 ◽  
Author(s):  
C Laurant ◽  
S D de Lauzon ◽  
N Cittanova ◽  
E Nunez ◽  
M F Jayle
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Rat Liver ◽  
Bovine Serum ◽  
Binding Proteins ◽  
Specific Binding ◽  
Naturally Occurring ◽  
Γ Globulins ◽  
Hydroxy Steroid ◽  
Steroid Dehydrogenase

1. The specificity of 3 oestradiol-binding proteins was studied. Two of these proteins are naturally occurring (rat α-foetoprotein and rat liver microsomal 17β-hydroxy steroid dehydrogenase) and the third is an artificially induced model, anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) γ-globulins. 2. A specific binding procedure for each protein model permitted a determination of its affinity for oestradiol and for 30 other steroids. 3. The results obtained have brought to light the different areas of the steroid molecule that are important for its recognition by each of the three proteins. The two naturally occurring proteins (α-foetoprotein and 17β-hydroxy steroid dehydrogenase) recognize the edge of the steroid defined by C-4, C-6, C-8 and C-15. On the other hand, the γ-globulins recognize the opposite edge, i.e. that defined by C-2, C-10, C-11 and C-17. 4. Diethylstilboestrol, whose structure is analogous to that of a steroid, is only recognized by the two naturally occurring proteins.

Stable near-infrared photoluminescence from silicon quantum dot–bovine serum albumin composites

2020 ◽  
Vol 10 (4) ◽  
pp. 680-686
Author(s):  
Asuka Inoue ◽  
Hiroshi Sugimoto ◽  
Yozo Sugimoto ◽  
Kensuke Akamatsu ◽  
Marie Hubalek Kalbacova ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Quantum Dot ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Near Infrared ◽  
Silicon Quantum Dot

Abstract

THE BINDING OF ETHACRYNIC ACID TO BOVINE SERUM ALBUMIN

1967 ◽  
Vol 45 (9) ◽  
pp. 1433-1443 ◽  
Author(s):  
Edward Ronwin ◽  
Anthony G. Zacchei
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Plasma Protein ◽  
Binding Sites ◽  
Bovine Serum ◽  
Concentration Ratio ◽  
Ethacrynic Acid ◽  
Specific Binding ◽  
Albumin Fraction ◽  
Specific Binding Sites

Studies with 14C-labelled ethacrynic acid indicated that this potent diuretic binds to the albumin fraction of plasma protein. An investigation of the variation of molar binding as a function of the molar concentration ratio revealed that a mole of bovine serum albumin can bind 4 moles of ethacrynic acid strongly (probably irreversibly) and approximately 12 moles reversibly at pH 7.4. Further, it appears that the protein could accommodate a maximum of approximately 16 reversibly bound moles of ethacrynic acid at this pH. Efforts to determine the chemical identity of specific binding sites did not allow positive assignments.

scholarly journals STUDY ON ANTIOXIDANT, ANTI-INFLAMMATORY AND HEPATOPROTECTIVE ACTIVITIES ON CARBON TETRACHLORIDE – INDUCED HEPATIC DAMAGE IN MICE OF TRANG TO (Ixora duffii) LEAF EXTRACT

2019 ◽  
Vol 41 (1) ◽  
Author(s):  
Dai Thi Xuan Trang
Keyword(s):  
Body Weight ◽  
Carbon Tetrachloride ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Leaf Extract ◽  
Hepatoprotective Activity ◽  
Control Group ◽  
Effective Reduction ◽  
Anti Inflammatory

Trang To (Ixora duffii) belongs to Ixora genus in the family Rubiaceae. The in vitro total antioxidant and anti-inflammatory capacity of Trang To methanol leaf extract was investigated by using phosphomolypdenum method and Bovine serum albumin denaturation test. The results have shown that Trang To methanol leaf extract possessed relatively high antioxidant activity, the value OD0,5 of Trang To (OD0,5 = 15,551 ± 0,344 μg / mL) was compared to that of the standard, trolox (OD0,5=2,315±0,083 μg/mL). The anti-inflammatory effect of Trang To leaf extract obtained in Bovine serum albumin denaturation test (EC50= 6,03±0,12μg/mL) was comparable to reference drugs, diclofenac sodium (EC50= 0,57±0,21µg/mL). The hepatoprotective activity of the methanol leaf extract of Trang To was investigated in mice which their livers were damaged by carbon tetrachloride (CCl4) mixed in olive oil (1: 4) at dose 2.5 mL/kg body weight/ day. The standard hepatoprotective agent is silymarin, was used at dose 16 mg/kg body weight during 4 consecutive weeks. The results of Trang To leaf extract was examined at three different doses 100, 200 and 400 mg/kg body weight all showed the effective reduction of transaminase enzyme levels in serum, with ALT levels (104,80±14,84 U/L, 84,20±20,02 U/L, 45,00±21,06 U/L) and AST levels (137,40±26,30 U/L, 119,20±6,40 U/L và 88,80±14,62 U/L) when increasing of the extract dose, respectively. In addition, Trang To leaf extract also improved the oxidative stress status in the liver through effective reduction of MDA level and increasing of GSH level in the liver. Observation of the microscopic cross section of liver tissue revealed that the mice treated with Trang To leaf extract had significantly improvement in liver tissues compared to the non-treated control group, these also showed similar results as silymarin at dose 16 mg/kg body weight. The results of this study demonstrated the efficacy of Trang To leaf extract in antioxidant and hepatoprotective activity.

Spectral investigations of the interaction of some porphyrins with bovine serum albumin

2000 ◽  
Vol 04 (02) ◽  
pp. 147-157 ◽  
Author(s):  
SHAMPA CHATTERJEE ◽  
T. S. SRIVASTAVA
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tertiary Structure ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Cd Studies

The binding of meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin (T4CPP), meso-tetrakis[3-(carboxymethyleneoxy)phenyl]porphyrin (T3CPP) and meso-tetrakis[3,4-bis(carboxymethyl-eneoxy)phenyl]porphyrin (T3, 4BCPP) with bovine serum albumin (BSA) at pH 7.4 has been studied at 420 nm in detail. The results show hypochromicity along with a red shift in the Soret band of the porphyrins. This suggests that these porphyrins bind to BSA as monomers. Further analysis of these data supports the non-interactive binding of T4CPP and T3CPP with BSA and the cooperative binding of T3, 4BCPP with BSA. These binding data have been interpreted in terms of one specific binding site and several non-specific binding sites on BSA for the porphyrins. The absorption spectral changes of the porphyrins between 400 and 450 nm when titrated with BSA suggest that there is another specific binding site on BSA for the porphyrins. These two specific binding sites have also been supported by circular dichroism (CD) studies. The absorption spectral and CD studies on the interactions of the porphyrins with BSA further suggest that these interactions are dependent on the number and configuration of substituents in the phenyl groups of the porphyrins. The contact energy transfer from the aromatic amino acid residues tryptophan and tyrosine of BSA to the porphyrins in the BSA–porphyrin complexes has also been studied using fluorescence spectroscopy. These energy transfer data show the energy transfer from tryptophan to the porphyrins for their binding to site I of BSA and from tyrosine to the porphyrins for their binding to site II of BSA. Unfolding studies of the BSA–porphyrin systems indicate that the tertiary structure is essential for the binding of the porphyrins. A correlation between the accumulation of99 mTc -labelled T4CPP and T3, 4BCPP in tumour tissue and their binding at site II of BSA is possible. The interaction of the porphyrins can also be used as a model for mitochondrial interactions.

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