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Biomedical subjects

F F Bolander

Publications and source records attributed to F F Bolander.

46 records · Page 3Linked to original sources
PubMed1978

Evidence for a hypothalamic defect in septo-optic dysplasia.

A 21-year-old man demonstrated septo-optic dysplasia. Optic and retinal colobomas were present and panhypopituitarism was documented. Releasing hormone studies showed partial luteinizing hormone (LH) response and no follicle-stimulating hormone response to administration of gonadorelin (LH-releasing hormone); thyroid-stimulating hormone (TSH) and prolactin levels were increased normally after administration of protirelin (thyrotropin-releasing hormone). The LH, TSH, and prolactin responses are believed to be evidence of intact pituitary function and suggest that a hypothalamic defect accounts for the hypopituitarism.

Adult↗
PubMed1976

The purification and characterization of rabbit placental lactogen.

Rabbit placental lactogen, a polypeptide hormone functionally related to the growth hormone/prolactin family, was isolated from placenta by (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography on DEAE-and CM-cellulose. The hormone was purified to more than 90% homogeneity, as determined by end-group analysis. On disc gel electrophoresis at pH9.0 it migrates as a pair of closely spaced bands with mobilities of 0.489 (minor band) and 0.511 (major band), and its isoelectric point is 6.1. Its mol.wt. is 20600, as determined by sedimentation--equilibrium centrifugation, and 24200, as estimated by gel electrophoresis in sodium dodecyl sulphate. Its amino acid composition resembles that of rabbit growth hormone and rat prolactin, except for a lower glutamic acid and leucine content. Like the prolactins, rabbit placental lactogen has two tryptophan and six cysteine residues, and its N-terminus, valine, is identical with that for human placental lactogen. By radioimmunoassay, it does not cross-react with antisera to either rat growth hormone or rat prolactin; in addition, it does not cross-react with antisera to bovine placental lactogen by double immunodiffusion. The similarity of the biochemical characteristics of rabbit placental lactogen to the other non-primate placental lactogens lends further support to the hypothesis that these molecules occupy a more central position in the growth hormone/prolactin "tree" than do their primate counterparts.

Amino Acids↗
PubMed1976

Purification and characterization of bovine placental lactogen.

Bovine placental lactogen (bPL), a polypeptide hormone functionally related to bovine growth hormone (bGH) and bovine prolactin (bPL), has been isolated from placentas by pH and ammonium sulfate precipitation, gel filtration, and ion exchange chromatography on DEAE- and CM-cellulose. The hormone has been purified to approximately 99% homogeneity, as determined by end group analysis. On disc gel electrophoresis at pH 9.0 bPL migrates as a pair of closely spaced bands (Rf = 09517 and 0.541) between the positions of bGH and bPR. Its molecular weight, as estimated by gel filtration on Sephadex G-200 in 6 M guanidine hydrochloride and 6.5 mM dithiothreitol, is 22, 150 and its isoelectric point is 5.9. The amino acid composition of bPL closely resembles that of bGH and bPR except for a higher content of serine and glycine and a lower leucine content. Like bPR, it has 2 tryptophans and 6 cysteines, but its COOH-terminal sequence is identical with that of bGH: -Cys-Ala-Phe-OH. By Ouchterlony immunodiffusion, bPL forms lines of partial identity with bGH against bGH antisera and with ovine placental lactogen (oPL) against oPL antisera. In the bPL-antibPL system, oPL forms a line of partial identity while bGH and bPR do not cross-react. However, bPL does not form a precipitin line with bPR antisera. These data would indicate that in terms of structure, and hence molecular evolution, bPL and other subprimate placental lactogens occupy a position more intermediate between growth hormone and prolactin than do the primate placental lactogens.

Amino Acids↗
PubMed1976

Localization and specificity of binding of subprimate placental lactogen in rabbit tissues.

A search for specific placental lactogen binding was undertaken in tissues obtained from late pregnant rabbits using the placental lactogens from sheep, cows, and human beings. 125I-labeled ovine lactogen exhibited highest specific binding to the adrenal gland (57.8%), followed by liver (21.5%), ovary (19.9%), mammary gland (15.9%), uterus (12.2%), kidney (8.8%), brain (8.5%), and adipose tissue (7.9%). In liver and mammary gland, the displacement curves for ovine and human lactogen were identical to that for bovine prolactin, indicating that they share the same receptor site. Although the displacement curve for bovine lactogen was parallel to that of the other lactogens the bovine hormone is less active in the radioreceptor assay.

Adrenal Glands↗
PubMed1976

Circulating placental lactogen levels in dairy and beef cattle.

Levels of bovine placental lactogen (bPL) have been measured in the serum of dairy and beef cattle and in the milk and amniotic fluid of pregnant animals with a highly specific radioimmunoassay. In both dairy and beef cows, serum bPL levels remain low (less than 50 ng/ml) during the first two trimesters and then rise rapidly between 160 and 200 days of gestation to a plateau. The bPL levels do not decline prior to parturition. During the last trimester, serum levels in dairy cows, 1103+/-342 ng/ml, are significantly higher than those in beef cattle, 650+/-37 ng/ml (P less than 0.01); furthermore, dairy cows having a high milk production also tend to have high bPL levels. Serum levels are almost twice as high in twin pregnancies and are not correlated with fetal sex or birth weight. bPL levels in milk and amniotic fluid from dairy cattle during the last trimester are approximately 86% and 25% of the serum values, respectively, suggesting that bPL enters these fluids by passive diffusion.

Amniotic Fluid↗
PubMed1975

Growth hormone covalently bound to sepharose or glass. Analysis of ligand release rates and characterization of soluble radiolabeled products.

Purified boveine growth hormone labeled enzymatically with iodine-125 was covalently coupled to cyanogen bromide activated Sepharose 4B gel and to diazotized zirconia-clad glass beads. Under the conditions employed, an average of 0.8 and 7.3 mg of hormone were bound per ml of Sepharose and glass, respectively. When the conjugates were incubated in Krebs-Ringer bicarbonate buffer (pH 7.4), three separate radioactive species were detected in the incubation supernatant by chromatography on Sephadex G-75. The elution volumes of two of the species were identical with those of 125-I-labeled growth hormone and Na-125I controls, while the third component eluted as a moleucle of intermediate size. The rate of release of each species from the solid matrix was linear with time over 4 days and increased with temperature from 4 to 37 degrees. Although significantly less growth hormone was released from glass (0.14%/day) than from Sepharose (0.40%/day) at 37 degrees, active hormone in amounts sufficient to be detectable in a biological assay was nevertheless liberated from the former after as little as 4 hr of incubation. By contrast, the rate of release of 125-Iminus- and the intermediate-size compound from glass was significantly greater than from Sepharose, suggesting that protein bound to glass supports is more susceptible to degradation from exposure to ionizing radiation.

Animals↗