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 Uptake of fluorescent-labeled BSA into root cells: endocytosis?

2014 ◽  
Vol 66 (3-4) ◽  
pp. 319-324 ◽  
Author(s):  
A. Kaźmierczak ◽  
J. Maszewski
Keyword(s):  
Zea Mays ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cytochalasin B ◽  
Fluorescein Isothiocyanate ◽  
Cell Type ◽  
Root Cells ◽  
Root Zones ◽  
Species Specific

Incorporation of rhodamine- and fluorescein-isothiocyanate labeled bovine serum albumin (BSA-TRITC, BSA-FITC) was examined in different root zones of the 3-day-old seedlings in <em>Melandrium noctiflorum</em>, <em>Allium cepa</em> and <em>Zea mays</em>. The uptake of fluorescent-labeled BSA was found: (1) species-specific, (2) cell-type dependent, and (3) cytochalasin B-sensitive. The characteristic punctute distribution of vesicles within the cytoplasm suggests the internalization of labeled proteins by endocytosis.

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.

scholarly journals Self-assembled bovine serum albumin nanoparticles as pesticide delivery vectors for controlling trunk-boring pests

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Chenyu Su ◽  
Shanshan Liu ◽  
Shenghan Cao ◽  
Shuyan Yin ◽  
Chenggang Zhou ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Bovine Serum ◽  
Fluorescein Isothiocyanate ◽  
Effective Control ◽  
Transport Efficiency ◽  
Dead Trees ◽  
Self Assembled ◽  
And Control

Abstract Background Trunk-boring pests (TBPs) are an important type of forest pest, TBPs not only feed on the branches and trunks of trees, but also spread quarantine diseases in forests. However, because the larvae of TBPs live inside the trunk and are well concealed, prevention and control are difficult. The lack of effective control methods leads to the death of many trees in forests. In this study, a novel nanopesticide featuring high bioactivity and slow-release properties was developed to control TBPs. Thiacloprid (THI), which is commonly used to control Coleoptera species, was used as a model pesticide. Results The oleophobic properties of bovine serum albumin (BSA) were exploited to encapsulate the hydrophobic pesticide THI by self-assembly, and the size of the obtained nanoparticles, THI@BSA·NPs, was approximately 23 nm. The loading efficiency reached 70.4%, and THI@BSA·NPs could be released continuously for over 15 days, with the cumulative release reaching 93.5%. The fluorescein isothiocyanate (FITC)-labeled nanoparticles were evenly distributed in the digestive tract and body surface of a typical TBPs, M. alternatus, and the stomach and contact toxicities increased by 33.7% and 25.9%, respectively, compared with those of free THI. Furthermore, the results showed that the transport efficiency of THI@BSA·NPs was highest at a concentration of 50 μg/mL, and the THI@BSA·NPs content in the trunk, from to lower to higher layers, was 8.8, 8.2, 7.6, and 5.8 μg/g. At the same time, THI@BSA·NPs also exhibited high transport efficiency in dead trees. Conclusion The transport efficiency and toxicity of the active ingredients are the key factors for the control of TBPs. This work provided idea for the application of biological delivery system encapsulated hydrophobic pesticides. The novel self-assembled THI@BSA·NPs have promising potential for sustainable control of TBPs.

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.

scholarly journals Self-Assembled Bovine Serum Albumin Nanoparticles as Pesticide Delivery Vectors for Controlling Trunk-Boring Pests

2020 ◽  
Author(s):  
Chenyu Su ◽  
Shanshan Liu ◽  
Shenghan Cao ◽  
Shuyan Yin ◽  
Chenggang Zhou ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Bovine Serum ◽  
Fluorescein Isothiocyanate ◽  
Effective Control ◽  
Transport Efficiency ◽  
Dead Trees ◽  
Self Assembled ◽  
And Control

Abstract Trunk-boring pests (TBPs) are an important type of forest pest, TBPs not only feed on the branches and trunks of trees, but also spread quarantine diseases in forests. However, because the larvae of TBPs live inside the trunk and are well concealed, prevention and control are difficult. The lack of effective control methods leads to the death of many trees in forests. In this study, a novel nanopesticide featuring high bioactivity and slow-release properties was developed to control TBPs. Thiacloprid (THI), which is commonly used to control Coleoptera species, was used as a model pesticide. The oleophobic properties of bovine serum albumin (BSA) were exploited to encapsulate the hydrophobic pesticide THI by self-assembly, and the size of the obtained nanoparticles, THI@BSA·NPs, was approximately 23 nm. The loading efficiency reached 70.4%, and THI@BSA·NPs could be released continuously for over 15 d, with the cumulative release reaching 93.5%. The fluorescein isothiocyanate (FITC)-labeled nanoparticles were evenly distributed in the digestive tract and body surface of a typical TBP, M. alternatus , and the stomach and contact toxicities increased by 33.7% and 25.9%,respectively, compared with those of free THI. Furthermore, the results showed that the transport efficiency of THI@BSA·NPs was highest at a concentration of 50 μg/mL, and the THI@BSA·NPs content in the trunk, from to lower to higher layers, was 8.8, 8.2, 7.6, and 5.8 μg/g. At the same time, THI@BSA·NPs also exhibited high transport efficiency in dead trees. The results suggested that these novel self-assembled THI@BSA·NPs have promising potential for sustainable control of TBPs.

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.

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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