Enhanced in vitro hepatic glucuronidation of thyroxine in rats following cutaneous application or ingestion of polychlorinated biphenyls

1976 ◽  
Vol 54 (1) ◽  
pp. 23-26 ◽  
Author(s):  
C. H. Bastomsky ◽  
P. V. N. Murthy
Keyword(s):  
Protein Concentration ◽  
Polychlorinated Biphenyl ◽  
Liver Weight ◽  
Mineral Oil ◽  
Supernatant Fluid ◽  
Purina Chow ◽  
Weight Protein ◽  
Liver Homogenates ◽  
Cutaneous Application

In rats four daily skin applications of a 30% solution of a polychlorinated biphenyl (PCB) mixture in mineral oil or of a microscope immersion oil, containing 34% PCB, led to increases in liver weight, protein concentration of the 10 000 × g supernatant fluid of liver homogenates and the in vitro glucuronidation of thyroxine (T4) by the supernatant fluid, whether related to liver weight or to protein concentration in the reaction mixture. Similar effects occurred after feeding 250 ppm (mg/kg) of PCB in either Purina chow or a low-iodine diet for 11 days. It is concluded that increased hepatic T4 glucuronidation contributes to the enhanced biliary excretion of T4 previously observed in PCB-treated rats.

The Effects of Haematocrit, Plasma Protein Concentration and Temperature of Drug-containing Blood In-vitro on the Concentrations of the Drug in the Plasma

1990 ◽  
Vol 42 (8) ◽  
pp. 577-580 ◽  
Author(s):  
AKIRA TAMURA ◽  
KAZUMOTO SUGIMOTO ◽  
TAKASHI SATO ◽  
TATSUZO FUJII
Keyword(s):  
Plasma Protein ◽  
Protein Concentration ◽  
Plasma Protein Concentration

scholarly journals Peroxidized mineral oil increases the oxidant status of culture media and inhibits in vitro porcine embryo development

2017 ◽  
Vol 103 ◽  
pp. 17-23 ◽  
Author(s):  
C.A. Martinez ◽  
A. Nohalez ◽  
J.J. Ceron ◽  
C.P. Rubio ◽  
J. Roca ◽  
...  
Keyword(s):  
Embryo Development ◽  
Culture Media ◽  
Mineral Oil ◽  
Porcine Embryo ◽  
Oxidant Status

scholarly journals Gastric secretion rate and protein concentration impact intragastric pH and protein hydrolysis during dynamic in vitro gastric digestion

2021 ◽  
Vol 1 ◽  
pp. 100027
Author(s):  
Yamile A. Mennah-Govela ◽  
Clay Swackhamer ◽  
Gail M. Bornhorst
Keyword(s):  
Gastric Secretion ◽  
Protein Concentration ◽  
Secretion Rate ◽  
Protein Hydrolysis ◽  
Intragastric Ph ◽  
Gastric Digestion

Substrate specificity of iodothyronine 5′-deiodinase in rat liver homogenates and its requirements of divalent cations in vitro

Life Sciences ◽  
1986 ◽  
Vol 38 (24) ◽  
pp. 2231-2238 ◽  
Author(s):  
Shinya Kobayshi ◽  
Yan Gao ◽  
Richard L. Ong ◽  
Constance S. Pittman
Keyword(s):  
Substrate Specificity ◽  
Rat Liver ◽  
Divalent Cations ◽  
Liver Homogenates

Ascorbate administration to normal and cholesterol-fed rats inhibits in vitro TBARS formation in serum and liver homogenates

Life Sciences ◽  
1996 ◽  
Vol 58 (14) ◽  
pp. 1101-1108 ◽  
Author(s):  
Mariarosaria Santillo ◽  
Paolo Mondola ◽  
Alfredo Milone ◽  
Anna Gioielli ◽  
Maurizio Bifulco
Keyword(s):  
Liver Homogenates ◽  
Tbars Formation

scholarly journals Automated analysis of filopodial length and spatially resolved protein concentration via adaptive shape tracking

2016 ◽  
Vol 27 (22) ◽  
pp. 3616-3626 ◽  
Author(s):  
Tanumoy Saha ◽  
Isabel Rathmann ◽  
Abhiyan Viplav ◽  
Sadhana Panzade ◽  
Isabell Begemann ◽  
...  
Keyword(s):  
Protein Concentration ◽  
Growth Dynamics ◽  
Automated Analysis ◽  
Cell Types ◽  
Control Mechanisms ◽  
Spatially Resolved ◽  
Novel Approach ◽  
Associated Proteins

Filopodia are dynamic, actin-rich structures that transiently form on a variety of cell types. To understand the underlying control mechanisms requires precise monitoring of localization and concentration of individual regulatory and structural proteins as filopodia elongate and subsequently retract. Although several methods exist that analyze changes in filopodial shape, a software solution to reliably correlate growth dynamics with spatially resolved protein concentration along the filopodium independent of bending, lateral shift, or tilting is missing. Here we introduce a novel approach based on the convex-hull algorithm for parallel analysis of growth dynamics and relative spatiotemporal protein concentration along flexible filopodial protrusions. Detailed in silico tests using various geometries confirm that our technique accurately tracks growth dynamics and relative protein concentration along the filopodial length for a broad range of signal distributions. To validate our technique in living cells, we measure filopodial dynamics and quantify spatiotemporal localization of filopodia-associated proteins during the filopodial extension–retraction cycle in a variety of cell types in vitro and in vivo. Together these results show that the technique is suitable for simultaneous analysis of growth dynamics and spatiotemporal protein enrichment along filopodia. To allow readily application by other laboratories, we share source code and instructions for software handling.

scholarly journals Studies on protein binding of antibiotics. IV. Effect of the binding of drug to 100,000*g supernatant fluid of rabbit liver homogenates on urinary excretion.

1982 ◽  
Vol 35 (11) ◽  
pp. 1603-1609
Author(s):  
YASUO WATANABE ◽  
RIEKO KITAYAMA ◽  
TOSHIO HAYASHI ◽  
YOSHIFUMI NAKASHIMA ◽  
MASASHI NOGUCHI ◽  
...  
Keyword(s):  
Protein Binding ◽  
Urinary Excretion ◽  
Rabbit Liver ◽  
Supernatant Fluid ◽  
Liver Homogenates

Polychlorinated biphenyl quinone exposure promotes breast cancer aerobic glycolysis: An in vitro and in vivo examination

2021 ◽  
pp. 127512
Author(s):  
Qi Qin ◽  
Bingwei Yang ◽  
Jing Liu ◽  
Erqun Song ◽  
Yang Song
Keyword(s):  
Breast Cancer ◽  
Polychlorinated Biphenyl ◽  
Aerobic Glycolysis

Biochemical studies of intrauterine components of the tammar wallaby Macropus eugenii during pregnancy

Development ◽  
1981 ◽  
Vol 62 (1) ◽  
pp. 325-338
Author(s):  
Elizabeth J. Thornber ◽  
Marilyn B. Renfree ◽  
Gregory I. Wallace
Keyword(s):  
Protein Concentration ◽  
Specific Binding ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fold Increase ◽  
Tammar Wallaby ◽  
Macropus Eugenii ◽  
Tenfold Increase ◽  
Specific Proteins ◽  
Wet Weight

The in vitro uptake and incorporation of [3H]ui idine by blastocysts of the tammar wallaby showed a 16- and 30-fold increase from day 0 to day 10 after removal of pouch young, respectively. Two of the six non-expanded blastocysts recovered on day 5 showed a tenfold increase in incorporation. During the first ten days after removal of pouch young the diameter of the blastocyst increased threefold. Endometrial exudate from gravid uteri had a higher protein concentration than exudate from nongravid uteri (39·5 ± 0·9 and 32·0 ± 2·0 mg/ml (mean ± s.e.m.), respectively). Endometrial exudates from uteri where the blastocyst was actively growing were found to contain six uterine-specific proteins. These were separated by gradient polyacrylamide gel electrophoresis. Two of the proteins were pre-albumins and the others were larger molecules (M.W. 153000–670000). Two proteins were only present at particular stages of pregnancy: the other four were present at all stages from diapause to birth, in exudate from gravid and nongravid uteri. The specific binding of progesterone and androstenedione to proteins in endometrial exudates or uterine flushings from pregnant wallabies was less than one per cent of the value obtained from day-5 pregnant rabbits. The ability of mouse blastocysts to take up and incorporate [3H]uridine into acidinsoluble material increased threefold in the presence of day-10 endometrial exudates from wallabies. However, this was less than ten percent of the values obtained in the presence of bovine serum albumin. The concentration of calcium in endometrial exudates increased from 23·6 to 45·2 μg/ml during pregnancy; in endometrium it remained at 88·7 μg/g (wet weight) throughout pregnancy, and in plasma it was 53·3 μg/ml. The concentration of zinc in endometrial exudates was 4·5 μg/ml; in endometrium it decreased from 21·8 to 13·3 μg/g (wet weight) during pregnancy and in plasma it was 0·6 μg/ml.

scholarly journals The assembly of microtubule protein in vitro. The kinetic role in microtubule elongation of oligomeric fragments containing microtubule-associated proteins

1985 ◽  
Vol 227 (2) ◽  
pp. 439-455 ◽  
Author(s):  
P M Bayley ◽  
F M M Butler ◽  
D C Clark ◽  
E J Manser ◽  
S R Martin
Keyword(s):  
Self Assembly ◽  
Protein Concentration ◽  
Wavelength Dependence ◽  
Electrophoretic Analysis ◽  
Slow Phase ◽  
Condensation Polymerization ◽  
Fast Phase ◽  
Microtubule Protein ◽  
Kinetics Of

The kinetics of assembly were studied for bovine and pig microtubule protein in vitro over a range of conditions of pH, temperature, nucleotide and protein concentration. The kinetics are in general biphasic with two major processes of similar amplitude but separated in rate by one order of magnitude. Rates and amplitudes are complex functions of solution conditions. The rates of the fast phase and the slow phase attain limiting values as a function of increasing protein concentration, and are more stringently limited at pH 6.5 than pH 6.95. Such behaviour indicates that mechanisms other than the condensation polymerization of tubulin dimer become rate-limiting at higher protein concentration. The constancy of the wavelength-dependence of light-scattering and ultrastructural criteria indicate that microtubules of normal morphology are formed in both phases of the assembly process. Electrophoretic analysis of assembling microtubule protein shows that MAP- (microtubule-associated-protein-)rich microtubules are formed during the fast phase. The rate of dissociation of oligomeric species on dilution of microtubule protein closely parallels the fast-phase rate in magnitude and temperature-dependence. We propose that the rate of this process constitutes an upper limit to the rate of the fast phase of assembly. The kinetics of redistribution of MAPs from MAP-rich microtubules may be a factor limiting the slow-phase rate. A working model is derived for the self-assembly of microtubule protein incorporating the dissociation and redistribution mechanisms that impose upper limits to the rates of assembly attainable by bimolecular addition reactions. Key roles are assigned to MAP-containing fragments in both phases of microtubule elongation. Variations in kinetic behaviour with solution conditions are inferred to derive from the nature and properties of fragments formed from oligomeric species after the rapid temperature jump. The model accounts for the limiting rate behaviour and indicates experimental criteria to be applied in evaluating the relative contributions of alternative pathways.

Sign in / Sign up

Export Citation Format

Share Document