FRACTIONATION OF 3–8S IODOCOMPOUNDS OF THE RAT THYROID

1971 ◽  
Vol 67 (2) ◽  
pp. 225-240 ◽  
Author(s):  
O. Spira ◽  
A. Gordon ◽  
J. Gross
Keyword(s):  
Serum Albumin ◽  
Electrophoretic Mobility ◽  
Half Life ◽  
Polyacrylamide Gel ◽  
Pool Size ◽  
Rat Serum ◽  
Rat Thyroid ◽  
Rat Serum Albumin

ABSTRACT The 3–8S iodocompounds of the rat thyroid were separated by means of electrodialysis on polyacrylamide gel columns into a dialyzable fraction (D) and non-dialyzable fraction (ND). The non-dialyzable fraction consisted of 4 peaks, one of which had the electrophoretic mobility of rat serum albumin. All 4 iodoproteins of the non-dialyzable fraction were shown in vitro to incorporate 3H-Leucine. The dialyzable fraction consisted of 6 iodine containing peaks, all of which incorporated 3H-Leucine. The half life and relative iodine pool size of each compound were determined and compared to the 19S thyroglobulin fraction.

scholarly journals A fluorescent residualizing label for studies on protein uptake and catabolism in vivo and in vitro

1990 ◽  
Vol 267 (1) ◽  
pp. 155-162 ◽  
Author(s):  
J L Maxwell ◽  
L Terracio ◽  
T K Borg ◽  
J W Baynes ◽  
S R Thorpe
Keyword(s):  
Half Life ◽  
Normal Tissue ◽  
Degradation Products ◽  
Rat Serum ◽  
Peripheral Tissues ◽  
Protein Uptake ◽  
Kinetics Of ◽  
Rat Serum Albumin

Residualizing labels are tracers which remain in lysosomes after uptake and catabolism of the carrier protein and have been especially useful for studies on the sites of plasma protein degradation. Thus far these labels have contained radioactive reporters such as 3H or 125I. In the present paper we describe a fluorescent residualizing label, NN-dilactitol-N′-fluoresceinylethylenediamine (DLF). Modification of asialofetuin (ASF) or rat serum albumin (RSA) with DLF affected neither their normal kinetics of clearance from the rat circulation nor their normal tissue sites of uptake and degradation. After injection of DLF-ASF, fluorescent degradation products were recovered nearly quantitatively in liver and retained with a half-life of about 2 days. Fluorescent degradation products from DLF-RSA were recovered in skin and muscle, and were localized in fibroblasts by fluorescence microscopy. These results confirm previous studies with radioactive residualizing labels in which fibroblasts in peripheral tissues were identified as primary sites of albumin degradation. Fluorescent catabolites also accumulated in fibroblasts incubated with DLF-RSA in vitro, and residualized with a half-life of about 2 days. Overall, the data establish that DLF functions efficiently as a fluorescent residualizing label both in vivo and in vitro. The advantages of fluorescent, compared with radioactive, residualizing labels should make them valuable tools for studies on protein uptake and catabolism in biological systems.

scholarly journals LABELING WITH 14C AMINO ACIDS OF ALBUMIN-LIKE PROTEIN BY RAT LIVER RIBONUCLEOPROTEIN PARTICLES

1963 ◽  
Vol 16 (3) ◽  
pp. 471-481 ◽  
Author(s):  
Alexandra von der Decken
Keyword(s):  
Amino Acids ◽  
Serum Albumin ◽  
Cellulose Acetate ◽  
Electrophoretic Mobility ◽  
Rat Liver ◽  
Deae Cellulose ◽  
Rat Liver Microsomes ◽  
Rat Serum ◽  
Ribonucleoprotein Particles ◽  
Rat Serum Albumin

Ribonucleoprotein particles were prepared by treatment of rat liver microsomes with detergents and high concentrations of KCl. They were active in incorporating 14C amino acids into protein when incubated with cell sap together with ATP, GTP, and a system to regenerate the triphosphates. The albumin of the incubation mixture, soluble at 105,000 g, and that of the fraction released by ultrasonication of the particles were studied by immunoelectrophoresis in agar gel. When the ribonucleoprotein particles were incubated with cell sap the immunological precipitation lines formed with antiserum to rat serum albumin were highly radioactive as tested by autoradiography. After zone electrophoresis on cellulose acetate, two immunologically reactive albumins were obtained which differed in their electrophoretic mobility from rat serum albumin. Labeled albumin, when purified on DEAE-cellulose columns, retained its radioactivity as tested by autoradiography following immunoelectrophoresis. On cellulose acetate this purified albumin showed an electrophoretic mobility higher than that of rat serum albumin.

scholarly journals Comparison of kinetic study of the photochemical changes of (ZZ)-bilirubin IXα bound to human serum albumin with that bound to rat serum albumin

1985 ◽  
Vol 230 (3) ◽  
pp. 561-567 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
T Yamakawa ◽  
K Isobe ◽  
M Manabe ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Rate Constants ◽  
Relative Rate ◽  
Rat Serum ◽  
Relative Rate Constants ◽  
Rat Serum Albumin

It has been stated by McDonagh, Palma & Lightner [(1982) J. Am. Chem. Soc. 104, 6867-6871] that complexing of bilirubin with serum albumin has a marked species-dependent influence on bilirubin photoisomerization in vitro and in vivo. Therefore the kinetics for the quantitatively important reaction: (Formula: see text) of the photochemical interconversion between bilirubin and its photoisomers bound to human or rat serum albumin in aqueous solution, assayed by h.p.l.c., was used to elucidate the observed species-dependent difference. The relative rate constants for bilirubin bound to human serum albumin, except for k4, the rate of interconversion from (ZZ)-bilirubin into (EZ)-bilirubin, proved to be considerably larger than those for bilirubin bound to rat serum albumin. In accordance with these rate constants, the formation of photoisomers of bilirubin bound to human serum albumin, except for (EZ)-bilirubin, is very rapid and much greater than that for bilirubin bound to rat serum albumin.

scholarly journals Experimental Approaches and Computational Modeling of Rat Serum Albumin and Its Interaction with Piperine

2019 ◽  
Vol 20 (12) ◽  
pp. 2856 ◽  
Author(s):  
Gabriel Zazeri ◽  
Ana Paula Ribeiro Povinelli ◽  
Marcelo de Freitas Lima ◽  
Marinônio Lopes Cornélio
Keyword(s):  
Serum Albumin ◽  
Well Being ◽  
Piper Nigrum ◽  
Computational Techniques ◽  
Spectroscopic Techniques ◽  
Rat Serum ◽  
Therapeutic Trials ◽  
Experimental Approaches ◽  
Rat Serum Albumin

The bioactive piperine (1-piperoyl piperidine) compound found in some pepper species (Piper nigrum linn and Piper sarmentosum Roxb) has been shown to have therapeutic properties and to be useful for well-being. The tests used to validate these properties were performed in vitro or with small rats. However, in all these assays, the molecular approach was absent. Although the first therapeutic trials relied on the use of rats, no proposal was mentioned either experimentally or computationally at the molecular level regarding the interaction between piperine and rat serum albumin (RSA). In the present study, several spectroscopic techniques were employed to characterize rat serum albumin and, aided by computational techniques, the protein modeling was proposed. From the spectroscopic results, it was possible to estimate the binding constant (3.9 × 104 M−1 at 288 K) using the Stern–Volmer model and the number of ligands (three) associated with the protein applying interaction density function model. The Gibbs free energy, an important thermodynamic parameter, was determined (−25 kJ/mol), indicating that the interaction was spontaneous. This important set of experimental results served to parameterize the computational simulations. The results of molecular docking and molecular dynamics matched appropriately made it possible to have detailed microenvironments of RSA accessed by piperine.

THE SECONDARY ANTIBODY RESPONSE IN TISSUE CULTURE: II. DIFFERENCES IN THE COURSE OF ANTIBODY SYNTHESIS TO DIPHTHERIA TOXOID AND RAT SERUM ALBUMIN

1965 ◽  
Vol 43 (6) ◽  
pp. 803-809 ◽  
Author(s):  
A. Juhasz ◽  
M. Richter
Keyword(s):  
Tissue Culture ◽  
Serum Albumin ◽  
Diphtheria Toxoid ◽  
Secondary Response ◽  
Antibody Synthesis ◽  
Rat Serum ◽  
Rat Serum Albumin ◽  
Footpad Injection ◽  
Secondary Stimulus

Lymph node fragments taken from rabbits previously immunized by a single footpad injection of both rat serum albumin and diphtheria toxoid were exposed to a secondary stimulus with either of these two antigens in vitro. The resulting secondary response was followed in tissue culture for a month. A difference was established in the antibody responses to rat albumin and diphtheria toxoid. Anti-diphtheria antibody formation was found to be more sensitive to hydrocortisone and less dependent on the presence of serum in the medium.

scholarly journals Biosynthesis of Rat serum albumin

1971 ◽  
Vol 123 (4) ◽  
pp. 649-655 ◽  
Author(s):  
J. D. Judah ◽  
Marion R. Nicholls
Keyword(s):  
Amino Acid ◽  
Serum Albumin ◽  
Time Course ◽  
Time Lag ◽  
Rat Serum ◽  
Albumin Content ◽  
Double Label ◽  
Rat Serum Albumin

1. The labelling of intracellular and extracellular serum albumin was studied in liver slices and in whole rats by using new methods for the purification of the protein. 2. The results suggest that a polypeptide precursor is formed that is converted relatively slowly into serum albumin. 3. The effect of liver cell K+has been examined by a double-label method and it is shown that K+accelerates the rate of conversion of ‘precursor’ into albumin. The rate of transit of albumin across the cell membrane appears to be unrelated to the concentration of K+within the cell. 4. The time-course of incorporation of radioactive amino acid into albumin follows a sigmoidal mode. There is a pronounced time-lag before label starts to appear in intracellular albumin, and a further time-lag before it appears in extracellular albumin. 5. In slices the sum of intra- and extra-cellular label rises steadily from 30min after the start of labelling with a pulse of labelled leucine or valine and continues to rise for at least another 60min. This occurs whether labelling is stopped by addition of excess of carrier amino acid or with cycloheximide (100μm) or both. 6. The intracellular albumin content remains constant whether slices are maintained with low or normal intracellular K+concentrations. 7. Specific radioactivities of intracellular albumin (and fractions thereof) and of extracellular albumin were determined in vitro and in vivo. The results show that the intracellular albumin cannot be a precursor of extracellular albumin, unless a very small compartment is turning over much more rapidly than the bulk of the liver albumin or even of the microsomal albumin.

scholarly journals The Biosynthesis of Rat Serum Albumin

1972 ◽  
Vol 247 (12) ◽  
pp. 3858-3863 ◽  
Author(s):  
Theodore Peters ◽  
James C. Peters
Keyword(s):  
Serum Albumin ◽  
Rat Serum ◽  
Rat Serum Albumin
Sign in / Sign up

Export Citation Format

Share Document