Radioimmunological and Chromatographic Properties of Tyrosine Methyl Ester Conjugates with Stereoisomeric Steroid Carboxy Derivatives

1996 ◽  
Vol 61 (5) ◽  
pp. 799-807 ◽  
Author(s):  
Oldřich Lapčík ◽  
Richard Hampl ◽  
Martin Hill ◽  
Luboslav Stárka ◽  
Alexander Kasal ◽  
...  
Keyword(s):  
Methyl Ester ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Hydroxy Group ◽  
Bovine Serum ◽  
The Other ◽  
Mixed Anhydride ◽  
Model Compounds ◽  
Binding Properties ◽  
Polyclonal Antisera

Pure 3Z (syn) and 3E (anti) stereoisomers of testosterone 3-[O-(2-carboxyethyl)]oxime were synthesized, separated by HPLC or TLC, and used for preparation of tyrosine methyl ester (TME) conjugates by using mixed anhydride or carbodiimide-N-hydroxysuccinimide methods. While the latter method provided more than 96% of product with retained configuration, the mixed anhydride method yielded a mixture containing 26-40% of the opposite stereoisomer. The stereoisomers were used as model compounds, to which the other steroid TMEs and the corresponding radioiodinated products could be aligned according to their chromatographic properties. The TME conjugates of 3-(O-carboxymethyl)oximes of seven 4-en-3-oxo steroids were further prepared by carbodiimide-N-hydroxysuccinimide method. With exception of cortisol, the stereoisomeric (Z and E) radioiodinated TME conjugates could be separated by TLC. In addition, the conjugates with TME and consequently radioiodinated tracers were synthesized from hemisuccinates of cortisol and its 11α-isomer, via 11β- and 11α-hydroxy group. The radioiodinated conjugates were tested as radioligands with rabbit polyclonal antisera raised by using position-homologous conjugates of the respective steroid carboxy derivatives with bovine serum albumin as immunogens. With the exception of 11-deoxycorticosterone, the stereoisomeric Z and E radioiodinated TMEs did not differ in their binding properties. In the case of isomeric cortisol tracers conjugated through position 11 the antisera recognized only the sterically homologous radioligands, but the specificity of the system was poor.

Trihalomethanes and haloacetic acid species from the chlorination of algal organic matter and bromide

2011 ◽  
Vol 63 (6) ◽  
pp. 1111-1120 ◽  
Author(s):  
Y. Y. Wei ◽  
Y. Liu ◽  
R. H. Dai ◽  
X. Liu ◽  
J. J. Wu ◽  
...  
Keyword(s):  
Organic Matter ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fish Oil ◽  
Microcystis Aeruginosa ◽  
Bovine Serum ◽  
Algal Species ◽  
Haloacetic Acid ◽  
Model Compounds ◽  
Reservoir Water

Bromide and algal pollution are important factors influencing disinfection byproduct (DBP) formation and speciation in reservoir water in coastal areas. In this study, the chlorination of model algal cellular compounds (bovine serum albumin, fish oil and starch), Microcystis aeruginosa and its extra-cellular organic matter (EOM) were conducted in the absence and presence of bromide. The main aim of the present study is to explore their potential as precursors for trihalomethanes (THMs) and haloacetic acid (HAAs) speciation upon chlorination in the presence of bromide. The results showed that all brominated THMs species were generated, whereas only bromochloroacetic acid (BCAA) or/and dibromoacetic acid (DBAA) was/were produced as for brominated HAAs (Br-HAAs) from the three model compounds in the presence of bromide. The effect of bromide on Br-HAAs speciation upon fish oil chlorination was more evident than with BSA and starch. There was a good correlation between the species predicted from the model compounds and those obtained from specific algal species. Br-HAAs and Br-THMs species from Microcystis aeruginosa cells or EOM were the same as those from bovine serum albumin in the presence of bromide.

scholarly journals Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin

1986 ◽  
Vol 236 (1) ◽  
pp. 307-310 ◽  
Author(s):  
M Y Khan
Keyword(s):  
Bovine Serum Albumin ◽  
Acid Solution ◽  
Serum Albumin ◽  
Protein Sequence ◽  
Bovine Serum ◽  
Direct Evidence ◽  
Structural Transformations ◽  
The Other ◽  
Ph Range ◽  
Domain Iii

The domain III of bovine serum albumin containing residues 377-582 of the protein sequence was isolated and its behaviour in acid solution was studied. The fragment was found to undergo structural transformations over the pH range 3.5-4.5 known to cause N-F transition in serum albumin. On the other hand, an albumin fragment that was devoid of domain III was unable to exhibit such a transition. These results were consistent with a mechanism where N-F transition involves the separation of domain III from the rest of the albumin starts at about pH 4.3 and is completed at pH 3.5.

The synthesis and investigation of binding properties of a new water soluble hexadeca zinc(ii) phthalocyanine with bovine serum albumin and DNA

2015 ◽  
Vol 39 (7) ◽  
pp. 5767-5775 ◽  
Author(s):  
Özge Kurt ◽  
İbrahim Özçeşmeci ◽  
B. Şebnem Sesalan ◽  
M. Burkut Koçak
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Binding Properties

The synthesis and the interaction between water soluble, non-aggregated, hexadeca substituted phthalocyanine zinc(ii) pc with DNA and BSA were reported.

RADIOIMMUNOASSAY OF THYROTROPHIN RELEASING HORMONE (TRH)

1974 ◽  
Vol 77 (3) ◽  
pp. 417-421 ◽  
Author(s):  
T. J. Visser ◽  
R. Docter ◽  
G. Hennemann
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
The Other ◽  
Thyrotrophin Releasing Hormone ◽  
Releasing Hormone ◽  
Double Antibody

ABSTRACT Immunization of rabbits with a conjugate in which L-pGlu-L-His-L-Pro-NH2 (TRH) at the amide side has been coupled to bovine serum albumin (BSA) yielded anti-TRH antibody which was detected by reaction of diluted antiserum with 3H-TRH. A double antibody radioimmunoassay has been developed in which 100 pg unlabelled TRH could be detected. Several analogues tested showed that only pGlu-His-Pro-OMe possessed comparable reactivity, while all the other compounds exhibited very little activity in the assay.

Sign in / Sign up

Export Citation Format

Share Document