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 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.

Screening radioimmunoassay for aldosterone in preheated plasma without extraction and chromatography.

1980 ◽  
Vol 26 (1) ◽  
pp. 41-45
Author(s):  
T M Connolly ◽  
L Tibor ◽  
K H Gless ◽  
P Vecsei
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Proteins ◽  
Equilibrium Dialysis ◽  
Screening Method ◽  
Plasma Aldosterone ◽  
Plasma Samples ◽  
Bovine Serum Albumin Conjugate ◽  
Native Plasma

Abstract We directly estimated plasma aldosterone radioimmunologically with use of an antiserum raised against an aldosterone-3-oxime/bovine serum albumin conjugate, the estimation being on samples with and without heating (60 degrees C), and diluted and undiluted. Values so obtained were compared with those by radioimmunoassay after extraction and chromatography. The correlation--even negative values were obtained--was poorest when the steroid was directly estimated in nonheated, undiluted plasma. Correlations were best (r = 0.918) for preheated and diluted native plasma, and the interassay CV was 9.8% (n = 57). However, there were some extraordinarily high values. After equilibrium dialysis of native and preheated (60 degrees C) plasma (15 plasma samples), the percentages of apparent free aldosterone and cortisol increased from 51.4 +/- 2.6% (SEM) to 64.3 +/- 1.6% and from 11.5 +/- 2.2% to 61.1 +/- 1%, respectively. We conclude that aldosterone-binding proteins play a role in direct radioimmunoassays of aldosterone in plasma, but by heating (with or without diluting) the plasma, direct assay can be used as a simple, fast, and inexpensive screening method.

Naturally occurring antibodies to bovine serum albumin in the parotid saliva of rats

1975 ◽  
Vol 20 (7) ◽  
pp. 415-418 ◽  
Author(s):  
T. Dishon ◽  
J. Sela ◽  
M. Ulmansky ◽  
E. Rosenmann ◽  
J.H. Boss
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Parotid Saliva ◽  
Naturally Occurring ◽  
Naturally Occurring Antibodies

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 Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin

2010 ◽  
Vol 02 (06) ◽  
pp. 563-570 ◽  
Author(s):  
Lucie Trnkova ◽  
Iva Bousova ◽  
Vladimir Kubicek ◽  
Jaroslav Drsata
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydroxycinnamic Acids ◽  
Naturally Occurring

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

2015 ◽  
Vol 6 (8) ◽  
pp. 2712-2726 ◽  
Author(s):  
Xin Peng ◽  
Xiangchao Wang ◽  
Wei Qi ◽  
Renliang Huang ◽  
Rongxin Su ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rosmarinic Acid ◽  
Acid Complex ◽  
Conformation Changes ◽  
Naturally Occurring

Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol. The interaction between bovine serum albumin and rosmarinic acid was studied to investigate the binding patterns and conformation changes.

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