scholarly journals Different characteristics of solubilized lactogen receptors from livers of pregnant and non-pregnant female rats

1982 ◽  
Vol 203 (3) ◽  
pp. 653-662 ◽  
Author(s):  
Norio Sasaki ◽  
Yuko Tanaka ◽  
Yasuo Imai ◽  
Toshio Tsushima ◽  
Fukashi Matsuzaki
Keyword(s):  
Binding Capacity ◽  
Pregnant Female ◽  
Female Rats ◽  
Scatchard Analysis ◽  
Female Rat ◽  
Binding Studies ◽  
Pregnant Rats ◽  
Pregnant Rat ◽  
Stokes Radius ◽  
Rat Livers

Receptors specific for lactogenic hormones were solubilized by 1% (v/v) Triton X-100 from the crude particulate membrane fraction of livers of pregnant and non-pregnant female rats and the characteristics of both preparations were compared. Human 125I-labelled somatotropin was used for binding studies of lactogenic hormone. The solubilized receptor retained most of the characteristics noted in the particulate fraction. The binding of human 125I-labelled somatotropin to the solubilized receptor is a saturable process, depending on temperature and time. Scatchard analysis of displacement curves revealed similar affinity constants ranging from 1.02 × 109 to 1.20 × 109 1/mol, while the binding capacity was 4.5 times greater in the pregnant rat livers than in the non-pregnant female rat livers. The receptors for human 125I-labelled somatotropin from livers of non-pregnant and pregnant female rats were equally adsorbed onto a concanavalin-A-Sepharose column and were dissociated from the column with α-methyl-d-glucoside or α-methyl-d-mannoside in the same manner. By gel filtration on Sepharose 6B, however, the molecular sizes of the hepatic receptors were found to be different. The apparent Mr value was approx. 270000 with a Stokes‘ radius of 5.5nm in the non-pregnant female rats and approx. 330000 with a Stokes’ radius of 5.5nm in the pregnant rats. Furthermore, isoelectric-focusing experiments showed that a major part of the receptor from the non-pregnant female rat livers had a neutral pI (7.0—8.5), whereas that from pregnant-rat livers had an acidic pI (4.2—4.7). These data suggest that the increase in the lactogenic binding capacity in rat liver membranes during pregnancy may be associated with marked changes of the physicochemical properties of the receptors.

PLASMA PROLACTIN AND PROGESTERONE RESPONSES TO MATING ARE ALTERED IN AGED RATS

1981 ◽  
Vol 90 (2) ◽  
pp. 179-191 ◽  
Author(s):  
S. HENDRICKS ◽  
C. A. BLAKE
Keyword(s):  
Plasma Concentrations ◽  
External Jugular Vein ◽  
Female Rats ◽  
Plasma Prolactin ◽  
Aged Rats ◽  
Pregnant Rats ◽  
Pregnant Rat ◽  
Plasma Progesterone ◽  
The One ◽  
The Right

The effects of varying amounts of copulatory stimulation on patterns of plasma concentrations of prolactin and progesterone were evaluated in 3- and 12-month-old female rats. The 12-month-old group included rats which still exhibited oestrous cycles and rats in persistent vaginal oestrus (PVO). The extent of copulatory stimulation was defined by the number of intromissions received during mating: ≤5,15 or > 50. Blood samples were drawn over the 8 days after mating through a cannula inserted into the right external jugular vein. Plasma from the samples was assayed for prolactin and progesterone. In aged but still cyclic rats, pregnancy rates were positively correlated with the number of intromissions received during mating. Only one rat in PVO became pregnant. All animals which became pregnant and rats in PVO which, after mating, exhibited a disruption of the pattern of PVO, showed the nocturnal surge of plasma prolactin characteristic of pregnant and pseudopregnant rats. While these surges persisted until day 8 after mating in pregnant animals, they were absent by this time in the rats in PVO. Prolactin surges were present in some but not all of the aged rats which did not become pregnant. Progesterone concentrations were raised in all pregnant animals except the one pregnant rat in PVO and, while not related to the number of intromissions, concentrations were higher 8 days after mating in young compared with those in aged pregnant rats. Plasma progesterone was low in rats in PVO regardless of disruption of the pattern of PVO. We have concluded that the failure of limited copulatory stimulation to induce pregnancy in older rats results, at least in part, from its failure to initiate nocturnal prolactin surges. Nevertheless, our data suggest that matings which are not experimentally limited should provide ample stimulation to establish such surges. Although reduced plasma concentrations of prolactin and progesterone at pro-oestrus and reduced plasma progesterone through part of gestation may contribute to decreasing fertility in aged rats, other unidentified factors appear to be involved in mediating the capacity of extensive copulatory stimulation to induce pregnancy in these animals.

scholarly journals Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

1995 ◽  
Vol 308 (1) ◽  
pp. 69-75 ◽  
Author(s):  
H I Yeh ◽  
C H Hsieh ◽  
L Y Wang ◽  
S P Tsai ◽  
H Y Hsu ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Female Rats ◽  
Spectrometric Analysis ◽  
Affinity Column ◽  
Female Rat ◽  
Significant Difference ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Molecular Masses ◽  
Rat Livers

Cytosolic glutathione S-transferases (GSTs) from rat livers were purified using an S-hexylglutathione affinity column. The GST subunits were resolved by reverse-phase HPLC and their molecular masses were determined by electrospray mass spectrometry. The major hepatic GSTs detected were subunits 1, 1′, 2, 3 and 4, with molecular mass of 25,520, 25,473, 25,188, 25,782 and 25,571 Da respectively. Subunits 6, 7 and 10 are minor components, with molecular mass of 25,551, 23,308 and 25,211 Da respectively. Alternatively, the hepatic GSTs were purified using a glutathione affinity column. Subunits 1, 1′, 2, 8 and 10 were eluted from this column with GSSG, the oxidized form of glutathione. Subunit 8 has a molecular mass of 25,553 Da. The remaining proteins on the glutathione affinity column were removed with glutathione and S-hexylglutathione. Subunits 2, 3, 4 and 6 could be detected in the eluate. We could not detect any significant difference in molecular mass between GSTs isolated from male and female rat livers. Cytosolic GSTs were isolated from livers of buthionine sulphoximine-treated female rats for MS analysis. The molecular masses obtained were identical to those determined for the controls.

Burn-induced alterations in cardiac beta-adrenergic receptors

1992 ◽  
Vol 262 (5) ◽  
pp. H1585-H1591 ◽  
Author(s):  
T. M. Kaufman ◽  
J. W. Horton
Keyword(s):  
Guinea Pig ◽  
Guinea Pigs ◽  
Adrenergic Receptors ◽  
Burn Injury ◽  
Binding Capacity ◽  
Total Body Surface Area ◽  
Scatchard Analysis ◽  
Beta Adrenergic Receptors ◽  
Binding Studies ◽  
Beta Adrenergic

Previous studies in our laboratory have demonstrated that burn injury (45% total body surface area, 3rd-degree scald burn) diminishes contractile and relaxation function in the isolated perfused guinea pig heart. The mechanisms responsible for the burn-mediated dysfunction are not well understood. Therefore the purpose of this study was to examine the inotropic response to isoproterenol, a beta-adrenergic agonist, and burn-induced alterations in beta-adrenergic receptors (beta-AR) in adult guinea pig hearts. Isoproterenol dose-response curves were generated in isolated perfused hearts from sham-burned and burned guinea pigs. In addition, binding studies were performed using [125I]iodocyanopindolol on hearts from sham-burned and burned guinea pigs. Both the functional response and sensitivity to isoproterenol were significantly diminished 24 h after burn injury. beta-AR density (binding capacity, Bmax) and affinity were determined by Scatchard analysis. Agonist competition curves were performed in the presence or absence of 0.1 mM 5'-guanylyl imidodiphosphate. There was no difference in Bmax in membranes from sham-burned and burned hearts; however, the affinity of beta-AR was significantly decreased after burn injury compared with sham burn [dissociation constant = 32.5 +/- 1.9 (mean +/- SE), n = 10, vs. 26.7 +/- 1.7 pM, n = 10, P = 0.039]. Furthermore, the fraction of receptors in a high-affinity state (those functionally coupled to Gs protein) was significantly decreased after burn injury compared with sham burn (41.2 +/- 4.7%, n = 9, vs. 54 +/- 2%, n = 9, P = 0.023).(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Sex-Related Liver Injury Due to Alcohol Involves Activation of Kupffer Cells by Endotoxin

2000 ◽  
Vol 14 (suppl d) ◽  
pp. 129D-135D ◽  
Author(s):  
Ronald G Thurman
Keyword(s):  
Liver Injury ◽  
Kupffer Cells ◽  
Coupling Constants ◽  
Female Rats ◽  
Male Rat ◽  
Gadolinium Chloride ◽  
Female Rat ◽  
Ethanol Treatment ◽  
Necrosis Factor Alpha ◽  
Rat Livers

Females have a greater susceptibility to ethanol-induced liver injury than males. Females who drink ethanol regularly and have been overweight for 10 years or more are at greater risk for both hepatitis and cirrhosis than males, and females develop ethanol-induced liver injury more rapidly and with less ethanol than males. Female rats on an enteral ethanol protocol exhibit injury more quickly than males and have widespread fatty changes over a larger portion of the liver lobule. Moreover, levels of plasma endotoxin, intracellular adhesion molecule-1, free radical adducts, infiltrating neutrophils and nuclear factor kappa B are doubled in female rat livers compared with male rat livers after enteral ethanol treatment. Additionally, estrogen treatment in vivo increases the sensitivity of hepatic macrophages or Kupffer cells to endotoxin. Evidence has been presented that Kupffer cells are pivotal in the development of ethanol-induced liver injury. Destroying Kupffer cells with gadolinium chloride or decreasing bacterial endotoxin by sterilizing the gut with antibiotics inhibits early inflammation due to ethanol. Similar results have been obtained with anti-tumour necrosis factor-alpha antibody. These data pointed to the hypothesis that ethanol-induced liver injury involves elevations in circulating endotoxin concentrations leading to activation of Kupffer cells, which causes a hypoxia-reoxygenation injury. This theory has been tested using pimonidazole, a 2-nitroimidazole marker, to quantify hypoxia in downstream, pericentral regions of the hepatic lobule. After chronic enteral ethanol treatment, pimonidazole binding doubles. Enteral ethanol also increases free radicals detected with electron spin resonance. Radical adducts, with coupling constants such as alpha-hydroxyethyl radical, have been shown to arise from ethanol. Importantly, hypoxia and radical production detected in bile are also decreased by the destruction of Kupffer cells with gadolinium chloride. These data support the hypothesis that Kupffer cells contribute to the vital sex differences in liver injury caused by ethanol.

scholarly journals Evidence that non-covalent forces, thiol and disulphide groups affect the structure and binding properties of the prolactin receptor on hepatocytes from pregnant rats

1985 ◽  
Vol 228 (2) ◽  
pp. 383-390 ◽  
Author(s):  
K Yamada ◽  
D B Donner
Keyword(s):  
Growth Hormone ◽  
Binding Capacity ◽  
Prolactin Receptor ◽  
Sodium Dodecyl ◽  
Specific Effect ◽  
Scatchard Analysis ◽  
Pregnant Rats ◽  
Receptor Complexes ◽  
Affinity Labelling ◽  
Triton X

Incubation of hepatocytes from pregnant rats with dithiothreitol decreased specific 125I-prolactin (125I-prl) binding to such cells by about 20% relative to control. This was not due to a non-specific effect of dithiothreitol on the cell membrane, since reduction also altered the binding of prl to solubilized partially purified receptor. Exposure of hepatocytes to N-ethylmaleimide (6 mM) for periods as brief as 1 min decreased the subsequent specific binding of 125I-prl by more than 50%. N-Ethylmaleimide was less effective as an inhibitor of binding when applied after hepatocytes had been exposed to 125I-prl, binding being decreased by about 15%. Scatchard analysis demonstrated that the effect of N-ethylmaleimide resulted from loss of receptor-binding capacity without any substantial effect on the affinity of the prl receptor for hormone. Dithiothreitol diminished the affinity of lactogenic sites for prolactin without altering cellular binding capacity. These observations suggest that thiol and disulphide groups are present in the prl receptor and that these functional moieties regulate the formation and properties of prl receptor complexes. The species to which 125I-prl had bound were identified by affinity labelling. 125I-prl was covalently coupled into saturable complexes of Mr 65000 and 50000. 125I-human growth hormone (125I-hGH) was covalently incorporated into complexes of Mr 300 000, 220 000, 130 000, 65 000 and 50 000. Bovine growth hormone (bGH), but not prl, competed for 125I-hGH uptake into the 300 000-, 220 000- and 130 000-Mr complexes, indicating that these species were somatogenic. Prl, but not bGH, inhibited 125I-hGH uptake into 65 000- and 50 000-Mr complexes. This demonstrated that 125I-hGH in the presence of bGH could affinity-label lactogenic receptors. 125I-prl aggregates in Triton X-100, whereas 125I-hGH does not. Therefore lactogenic complexes to which 125I-hGH was bound in the presence of excess bGH were solubilized in Triton X-100 and characterized sequentially by gel filtration and affinity labelling. Prl receptors were eluted from columns of Sepharose 6B as a species of Mr380 000. Fractionation of the 380 000-Mr species on sodium dodecyl sulphate polyacrylamide gels resulted in the isolation of complexes of Mr 65 000 and 50 000. Thus non-covalent forces stabilize aggregates of the monomeric prolactin receptor.

A COMPARISON OF THE CONCENTRATION OF C14 IN THE TISSUES OF PREGNANT AND NONPREGNANT FEMALE RATS FOLLOWING THE INTRAVENOUS ADMINISTRATION OF VITAMIN K1-C14 AND VITAMIN K3-C14

1957 ◽  
Vol 35 (1) ◽  
pp. 691-697 ◽  
Author(s):  
J. D. Taylor ◽  
G. J. Millar ◽  
R. J. Wood
Keyword(s):  
Skeletal Muscle ◽  
Vitamin K ◽  
Intravenous Administration ◽  
Fetal Liver ◽  
Live Weight ◽  
Fetal Tissue ◽  
Female Rats ◽  
Pregnant Rats ◽  
Pregnant Rat ◽  
Significant Difference

The C14 content was determined of the livers, spleens, skeletal muscle, blood, feces, and urine of both pregnant and nonpregnant female rats and of the placentas, fetal livers, fetuses, and amnionic fluids of pregnant rats following the intravenous administration of 5 mg./kg. of either vitamin K1-C14 or vitamin K3-C14. The C14 concentrations of the livers of the rats given vitamin Kt were about 24 times larger than those of animals that had received vitamin K3-C14. A fivefold difference in the same direction exists between the concentrations in the spleens of the two groups. The C14 levels for skeletal muscle, blood, placenta, fetal liver, and fetal tissue were of similar magnitude regardless of whether vitamin Kt or vitamin K3 was administered. Isotope dilution tests revealed that following intravenous administration of vitamin K1-C14 the amount of radioactivity present as unchanged vitamin Kt-C14 was 12% for fetal tissue, 59% for placenta, and 120% for the maternal liver. The dry weights of the livers of pregnant rats were larger than those of nonpregnant rats and the increase was proportional to the live weight of the pregnant rat. No significant difference could be demonstrated in the percentage of the injected dose of vitamin K1 deposited in the livers of pregnant or nonpregnant rats. The same was true for vitamin K3-C14. The results of this experiment indicate that vitamin K3-C14 is not concentrated in the liver of the rat whereas vitamin K1-C14 is. Furthermore, it would appear that both vitamin K1 and vitamin K3 can pass the placental barrier of the rat.

THE ROLE OF HORMONAL AND DIETARY FACTORS IN THE FORMATION OF EXCESS RIBONUCLEIC ACID IN THE LIVERS OF PREGNANT RATS

1953 ◽  
Vol 9 (1) ◽  
pp. 52-67 ◽  
Author(s):  
ROSA M. CAMPBELL ◽  
I. R. INNES ◽  
H. W. KOSTERLITZ
Keyword(s):  
Protein Content ◽  
Ribonucleic Acid ◽  
Liver Cells ◽  
Significant Rise ◽  
Dietary Factors ◽  
Pregnant Female ◽  
Female Rats ◽  
Liver Protein ◽  
Pregnant Rats ◽  
Dna And Rna

1. Excess ribonucleic acid ('RNA') is defined as the difference between the RNA contents of livers of pregnant and non-pregnant rats. Large amounts of excess RNA are formed in the liver of the rat during the last week of pregnancy. Excess RNA is formed in the liver after removal, on the 14th or 15th day of pregnancy, of the foetuses, or foetuses and ovaries, or foetuses and adrenals, or foetuses, ovaries and adrenals, or pituitary, or pituitary and foetuses, or pituitary, foetuses and ovaries. Viable placentae must be present. 2. Two fractions of RNA appear to be present in the liver cells of pregnant rats. One fraction varies linearly with the protein content of the liver cells, as does the RNA of non-pregnant rats' livers. The second fraction (excess RNA) is quite independent of the protein content of the liver cells but varies linearly with the weight of the placentae and the energy, but not the protein, content of the diet. 3. Hypophysectomy lowers the amount of excess RNA by 20–25 %. After removal of the foetuses on the 14th day, the placentae do not attain the normal weight, and the amount of excess RNA is smaller than in normal pregnancy. After removal of foetuses and ovaries the placentae are larger and heavier than after removal of the foetuses alone. 4. Both adrenalectomy and ovariectomy in non-pregnant female rats cause a small rise of liver deoxyribonucleic acid ('DNA') and RNA. After hypophysectomy, there is a loss in liver RNA greater than that expected from the simultaneous loss of liver protein. The loss of RNA occurs even when the loss of liver protein is prevented by feeding the rats by stomach tube. DNA is not lost from the liver a fortnight after hypophysectomy, as long as the energy intake is normal. 5. In non-pregnant female rats oestradiol, but not progesterone, causes an increase of liver DNA and RNA. This is not found in hypophysectomized rats. Injection of an alkaline placental extract causes a significant rise of liver RNA which, however, is very much smaller than that found in pregnancy. 6. Since hypophysectomy lowers, but does not abolish excess liver RNA in pregnant rats, it is concluded that at least two factors play a role: first and foremost, an unknown factor secreted by the placenta, acting independently of the pituitary, and second, increased amounts of oestrogen apparently requiring the presence of the pituitary.

THE PRESENCE OF LACTOGEN BUT NOT GROWTH HORMONE BINDING SITES IN THE ISOLATED RAT HEPATOCYTE

1977 ◽  
Vol 74 (2) ◽  
pp. 323-334 ◽  
Author(s):  
A. C. HERINGTON ◽  
N. M. VEITH
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Binding Sites ◽  
Specific Binding ◽  
Female Rats ◽  
Scatchard Analysis ◽  
Hormone Binding ◽  
Binding Studies ◽  
Membrane Function ◽  
Liver Membranes

The binding of 125I-labelled human growth hormone (hGH) and bovine growth hormone (bGH) has been studied in hepatocytes isolated from female rats by perfusion with collagenase in situ. The cells appeared to retain normal membrane function, in that amino acid ([14C]α-aminoisobutyric acid) transport was both saturable and temperature-dependent. Amino acid ([14C]leucine) incorporation into protein was also linear over 3 h and was inhibited by cycloheximide. Binding of 125I-labelled hGH was dependent on time, temperature, hepatocyte concentration and hGH concentration. At 22 °C, binding reached a steady-state after 2·5 h and had a half-life of dissociation of 2–3 h. Hormone specificity studies indicated that binding was specific for hormones with prolactin-like activity (hGH, prolactins) and not for growth hormones themselves (bGH). Scatchard analysis revealed a single class of binding site with a binding capacity of 26·74 ± 3·73 fmol/106 cells and a binding affinity of 1·24 × 109 ± 0·17 × 109 (s.e.m.) l/mol (n = 10). There was a significant sex difference in binding (female > male) and binding was subject to marked regulation by oestrogens (stimulation of binding) and by androgens (inhibition). The lactogen-binding sites, therefore, were comparable in many respects to those previously reported in rat liver membranes. No distinct GH binding sites were demonstrable as shown by the lack of specific binding by 125I-labelled bGH, purified either by Sephadex chromatography or by binding to and elution from GH receptors in rabbit liver membranes. The value of receptor purification of tracer for use in hormone binding studies was indicated by a substantial lowering of non-specific binding.

scholarly journals Characterization of the binding of human growth hormone to microsomal membranes from rat liver

1976 ◽  
Vol 158 (1) ◽  
pp. 61-69 ◽  
Author(s):  
A C Herington ◽  
N Veith ◽  
H G Burger
Keyword(s):  
Growth Hormone ◽  
Binding Site ◽  
Rat Liver ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Female Rats ◽  
Scatchard Analysis ◽  
Normal Female ◽  
Female Rat ◽  
Hormone Binding

The binding of 125I-labelled human growth hormone to the 100000g microsomal membrane fraction prepared from the livers of normal female rats was dependent on time, temperature, pH, membrane concentration and concentration of 125I-labelled human growth hormone. At 22 degrees C binding reached a steady state after 16h, with the mean maximal specific binding being 20% of the tracer initially added. Dissociation of 125I-labelled human growth hormone from the membranes, after addition of excess of unlabelled hormone, was relatively slow with a half-time greater than 24h. Only minor degradation of the 125I-labelled human growth hormone was observed during incubation with membranes for 16 or 25h at 22 degrees C. Similarly, no significant change in the ability of membranes to bind human growth hormone was evident after preincubation of the membranes for 16 or 25h. Specificity studies showed that up to 90% of the 125I-labelled human growth hormone bound could be displaced by 1 mug of unlabelled hormone. Ovine prolactin also showed considerable competition for the binding site. Non-primate growth-hormone preparations (ovine, bovine, porcine and rat) and non-related hormones (insulin, thyrotropin, lutropin and follitropin) all showed negligible competition. Scatchard analysis of the binding data was consistent with two classes of binding site with binding affinities of 0.64 × 10(10) +/- 0.2 × 10(10)M-1 and 0.03 × 10(10) +/- 0.007 × 10(10)M-1 and corresponding binding capacities of 98.4 +/- 10 fmol/mg of protein and 314.6 +/- 46.3 fmol/mg of protein. These studies provide data which, in general, are consistent with the criteria required for hormone-receptor interaction. However, proof of the thesis that the human-growth-hormone-binding sites in female rat liver represent physiological receptors must await the demonstration of a correlation between hormone binding and a biological response.

Age-related alterations in prolactin binding sites in the female rat

1991 ◽  
Vol 124 (3) ◽  
pp. 314-321 ◽  
Author(s):  
Philippe Schneiter ◽  
Marianne J. Reymond ◽  
Thérèse Lemarchand-Béraud
Keyword(s):  
Binding Sites ◽  
Mammary Glands ◽  
Female Rats ◽  
Affinity Constant ◽  
Female Rat ◽  
Binding Studies ◽  
Young Rats ◽  
Age Related ◽  
Old Rats ◽  
Nulliparous Female

Abstract. Aging is associated with various neuroendocrine alterations, including in the rat a hypersecretion of PRL with maintained ovulations (repetitive pseudopregnancy) and a reduced activity of the hypothalamic dopaminergic neurons with loss of the neuron responsiveness to PRL, suggestive of age-related alterations in PRL receptors. In this study we have investigated PRL binding sites in the hypothalamus as well as in the mammary glands, the ovaries and the liver of young and old nulliparous female rats. The old rats (26-28 months) displayed spontaneous repetitive pseudopregnancies and they were compared with young (4-6 months) pseudopregnant rats; the binding studies were performed by saturation analysis using 125I-oPRL as ligand and particulate membrane preparations. In the hypothalamus, a negligible binding of PRL was observed in all fragments studied, mediobasal hypothalamus, median eminence, in both young and old rats and no characterization of the binding sites could be achieved. In the mammary glands, the number of PRL binding sites was appreciable in spite of the nulliparity of the rats, but it was smaller in the old than in the young rats (9.0±1.4 vs 14.9±1.2 fmol/mg protein; mean ± sem; p<0.02). In the ovaries, the density of PRL binding sites was similar in the old and young rats (112.6±9.7 vs 115.0±8.9 fmol/mg protein), illustrative of a maintained luteotropic effect of PRL with age in the rat. In contrast, in the liver a greater number of binding sites was found in the old than in the young rats (261.9±36.6 vs 63.6±5.8 fmol/mg protein; p<0.001), supportive of the ability of PRL to induce its own receptors in that tissue. The affinity constant of PRL binding was not altered with age in the tissues studied. These results are illustrative of tissue-specific modifications in the number of PRL binding sites with age and they are suggestive of a sustained biological activity of PRL in the old rats.

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