scholarly journals Purification of the 22000- and 20000-mol.wt. forms of human somatotropin and characterization of their binding to liver and mammary binding sites

1983 ◽  
Vol 214 (3) ◽  
pp. 885-892 ◽  
Author(s):  
J Closset ◽  
J Smal ◽  
F Gomez ◽  
G Hennen
Keyword(s):  
Mammary Gland ◽  
Binding Capacity ◽  
Chemical Characterization ◽  
Rabbit Liver ◽  
Partial Agonists ◽  
Affinity Constants ◽  
Pregnant Rabbit ◽  
Maximum Binding Capacity ◽  
Specificity Of Binding

Quantitative data concerning the binding of 22000-mol.wt. human somatotropin and its 20000-mol.wt. variant are described using pregnant-rabbit liver and mammary-gland receptors. The purification and the complete chemical characterization of both human somatotropin and its 20000-mol.wt. variant is also presented. Contamination of the 20000-mol.wt.-variant preparation by 22000-mol.wt. hormone was found to be 0.5% by weight as measured in radioimmunoassay using monoclonal antibody. Labelling of human somatotropin and its 20000-mol.wt. variant using the Iodogen method is described as well as the characterization of the binding to pregnant-rabbit liver and mammary-gland receptor preparations. The maximum binding capacity of the 125I-labelled human somatotropin was between 50 and 60% to liver particulate receptor, whereas that of the 20000-mol.wt. variant was 30%. The specificity of binding of both forms to rabbit hepatic and mammary-gland receptor was found to be similar for both proteins in the same system. The affinity constants and capacity were respectively 0.7 X 10(10)M-1 and 815 fmol/mg of protein for human somatotropin and 0.6 X 10(10)M-1 and 1.250 fmol/mg of protein for the 20000-mol.wt. variant. These data suggest that both proteins behave as partial agonists to the receptors studied.

scholarly journals The specificity of binding of growth hormone and prolactin to purified plasma membranes from pregnant-rabbit liver

1986 ◽  
Vol 236 (3) ◽  
pp. 657-663 ◽  
Author(s):  
C F Webb ◽  
H F Cadman ◽  
M Wallis
Keyword(s):  
Growth Hormone ◽  
Plasma Membranes ◽  
Human Growth ◽  
Rabbit Liver ◽  
Complex Nature ◽  
Binding Properties ◽  
Microsomal Preparation ◽  
Pregnant Rabbit ◽  
Specificity Of Binding ◽  
Triton X

The binding of 125I-labelled human growth hormone (hGH) to a purified plasma membrane preparation from the liver of pregnant rabbit, and to receptors solubilized from this fraction with Triton X-100, was dependent on time, temperature, the cations used and the receptor concentration. Solubilization did not affect the binding properties of the receptors at low concentrations of Triton X-100. Some somatogenic hormones, such as bovine GH, and some lactogenic hormones, such as ovine prolactin, displaced 125I-labelled hGH from purified plasma membranes and solubilized receptor preparations, but GHs and prolactins from various other species were rather ineffective. The results indicate that although there are binding sites for hGH in these pregnant rabbit liver membranes, few of these are specifically somatogenic or lactogenic. The binding properties of the purified plasma membranes are similar to those of a microsomal preparation studied previously, suggesting that the complex nature of the binding of hGH is not due to the heterogeneity of cellular membranes used to study binding, but is a property of the receptors associated with plasma membranes.

Characterization of the growth hormone-binding protein of human serum using a panel of monoclonal antibodies

1989 ◽  
Vol 123 (2) ◽  
pp. 327-332 ◽  
Author(s):  
R. Barnard ◽  
P. Quirk ◽  
M. J. Waters
Keyword(s):  
Monoclonal Antibodies ◽  
Human Serum ◽  
Binding Capacity ◽  
Binding Protein ◽  
Cross Reactivity ◽  
Rabbit Liver ◽  
Rabbit Serum ◽  
Gh Receptor ◽  
Hormone Binding Protein

ABSTRACT A panel of monoclonal antibodies (MAbs) reactive with distinct epitopes on the rabbit liver GH receptor and rabbit serum GH-binding protein (GHBP) were tested for cross-reactivity with the GHBP from human serum. Four of seven MAbs reacted with the human serum GHBP. Immunoprecipitation of the human binding protein enabled hormonal specificity identical to that previously reported for human GH receptors to be demonstrated. Scatchard analyses of 125I-labelled human GH binding to the serum GHBP were carried out with correction made for endogenous human GH which was measured by radioimmunoassay of each serum sample. This approach yielded the first reliable estimates of the affinity and capacity of the human GHBP. The binding capacity (mean ± s.e.m.) of female sera (804±126 pmol/l; n= 6) was greater than that of male sera (505 ± 36 pmol/l; n=9; P < 0·02). The affinity of the GHBP was 0·91 ±0·10 litres/nmol (n= 15). The presence of multiple epitopes common to the human serum GHBP and the rabbit liver GH receptor is consistent with identity between the extracellular domains of the human GHBP and the human GH receptor, as is the case for the rabbit GHBP and GH receptor. Journal of Endocrinology (1989) 123, 327–332

Olfactory and Chemical Characterization of Indoor Air-Towards a Psychophysical Model for Air Quality

1981 ◽  
Author(s):  
Birgitta Berglund ◽  
Ulf Berglund ◽  
Thomas Lindvall ◽  
Helene Nicander-Bredberg
Keyword(s):  
Air Quality ◽  
Indoor Air ◽  
Chemical Characterization

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

Laboratory Methods for the Physico-Chemical Characterization of Recombinant Allergens as Reference Standards

Alergologia ◽  
2020 ◽  
Vol 1 (4) ◽  
pp. 7
Author(s):  
Mariana Vieru ◽  
Florin-Dan Popescu ◽  
Laura Haidar ◽  
Carmen Bunu-Panaitescu
Keyword(s):  
Chemical Characterization ◽  
Reference Standards ◽  
Recombinant Allergens ◽  
Laboratory Methods ◽  
Physico Chemical
Sign in / Sign up

Export Citation Format

Share Document