THE PREPARATION OF SHEEP GROWTH HORMONE

1963 ◽  
Vol 26 (2) ◽  
pp. 259-263 ◽  
Author(s):  
A. L. C. WALLACE ◽  
K. A. FERGUSON
Keyword(s):  
Growth Hormone ◽  
Anterior Pituitary ◽  
Deae Cellulose ◽  
Pituitary Hormones ◽  
Starch Gel Electrophoresis ◽  
Epiphysial Cartilage ◽  
Pituitary Glands ◽  
Hypophysectomized Rats ◽  
Starch Gel ◽  
Main Components

SUMMARY Growth hormone has been prepared from sheep pituitary glands by chromatography of a simple buffer extract on DEAE-cellulose. The preparation appears to be free of other anterior pituitary hormones but shows two main components when analysed by starch gel electrophoresis. These components appear similar to those present in standard preparations of ox growth hormone. Sheep growth hormone prepared by this method is not significantly less active than purified ox growth hormone when compared by the tibial-epiphysial cartilage response in hypophysectomized rats.

scholarly journals A chromatographic preparation of ox growth hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 593-600 ◽  
Author(s):  
M Wallis ◽  
HBF Dixon
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Highly Active ◽  
Cross Linkage ◽  
Starch Gel

1. A method is described for the chromatographic preparation of ox growth hormone. It involves chromatography of an extract of anterior pituitary lobes on DEAE-cellulose, followed by rechromatography on a dextran gel of low cross-linkage (Sephadex G-100). 2. The product is highly active in growth-hormone assays, and is obtained in good yield. It was homogeneous by several criteria, but showed some heterogeneity on starch-gel electrophoresis. 3. The molecular weight of the hormone was estimated from its behaviour on gel-filtration columns under various conditions. Evidence that the hormone may dissociate into sub-units under some conditions is presented.

IMMUNOLOGICAL STUDIES OF A BOVINE GROWTH HORMONE PREPARATION

1965 ◽  
Vol 32 (3) ◽  
pp. 321-327 ◽  
Author(s):  
A. L. C. WALLACE ◽  
W. R. SOBEY
Keyword(s):  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Active Components ◽  
Material Growth ◽  
Hypophysectomized Rats ◽  
Starch Gel ◽  
Growth Activity ◽  
Gel Diffusion

SUMMARY The NIH-B2-GH preparation of ox growth hormone (GH) was separated by chromatography on DEAE-cellulose into six fractions. Five of these fractions when assayed in hypophysectomized rats showed GH activity ranging in potency from 0·25 to 2·5 times the starting material. Growth activity could not be correlated with the concentration of any single component revealed by starch gel electrophoresis. Antisera produced to NIH-B2-GH had antihormone activity and produced two precipitin lines in Ouchterlony diffusion tests. One of these lines was associated with serum γ-globulin and was shared by all five fractions. The other line was present in only two of the fractions, and these contained the more anionic components. It is suggested that the more cationic growth-active components present in bovine and ovine GH preparations do not readily produce precipitating antibodies and that this may complicate the results of precipitin and gel diffusion tests when heterogeneous GH preparations have been used to prepare the antisera.

PURIFICATION OF FOLLICLE-STIMULATING HORMONE FROM HUMAN ANTERIOR PITUITARY GLANDS

1964 ◽  
Vol 42 (6) ◽  
pp. 841-849 ◽  
Author(s):  
W. H. McShan ◽  
B. B. Saxena ◽  
R. O. Creek
Keyword(s):  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Follicle Stimulating Hormone ◽  
Starch Gel Electrophoresis ◽  
Thyrotropic Hormone ◽  
Pituitary Glands ◽  
Starch Gel ◽  
Gonadotropic Activity ◽  
Human Anterior Pituitary ◽  
Stimulating Hormone

The results of this study indicate that highly purified follicle-stimulating hormone (FSH) was prepared from human anterior pituitary glands by ammonium sulphate (AS) fractionation, zone electrophoresis, and starch gel electrophoresis. The activity of this preparation was approximately 14.7 times that of the sheep pituitary FSH standard. The fractions from zone and starch gel electrophoresis with which luteinizing hormone (LH) was associated also contained thyrotropic hormone (TSH). There was little decrease in the gonadotropic activity of human anterior pituitary glands recovered at different times up to 24 hours post-mortem.

ELECTROPHORETIC SEPARATION OF HORMONES ASSOCIATED WITH SECRETORY GRANULES FROM RAT ANTERIOR PITUITARY GLANDS

1970 ◽  
Vol 63 (2) ◽  
pp. 378-384 ◽  
Author(s):  
D. R. Hodges ◽  
W. H. McShan
Keyword(s):  
Growth Hormone ◽  
Anterior Pituitary ◽  
Secretory Granules ◽  
Follicle Stimulating Hormone ◽  
Pituitary Hormones ◽  
Thyroid Stimulating Hormone ◽  
Disc Electrophoresis ◽  
Hormone Activity ◽  
Pituitary Glands ◽  
Stimulating Hormone

ABSTRACT Electrophoretic analyses of rat, mouse, human and cow anterior pituitary homogenates with subsequent bioassays for hormonal activity have been reported. Comparison of the behaviour of the hormonal activities from rat anterior pituitary secretory granules and that reported for pituitary homogenates was made following disc electrophoresis on polyacrylamide gels. Bioassays of gel segments for the six anterior pituitary hormones resulted in the localization of the activities of five of the six hormones. ACTH activity was not detected. Growth hormone and prolactin were associated with the major cathodal and anodal discs respectively. Luteinizing hormone and thyroid stimulating hormone activities had similar mobilities and were located in a zone just above growth hormone. The activity was not restricted to a discrete, stainable disc in either case. Follicle stimulating hormone activity was detected in a narrow segment containing only one disc a few millimeters below growth hormone. Comparison of the mobilities of the hormones from homogenates and secretory granule extracts suggests that they have essentially similar electrophoretic characteristics at basis pH.

THE CHROMATOGRAPHY ON DEAE-CELLULOSE OF PITUITARY EXTRACTS FROM SEVERAL SPECIES

1964 ◽  
Vol 30 (3) ◽  
pp. 387-397 ◽  
Author(s):  
A. L. C. WALLACE ◽  
K. A. FERGUSON
Keyword(s):  
Follicle Stimulating Hormone ◽  
Deae Cellulose ◽  
Pituitary Hormones ◽  
Thyroid Stimulating Hormone ◽  
Starch Gel Electrophoresis ◽  
Specific Nature ◽  
Starch Gel ◽  
Distribution Of Components ◽  
Species Specific ◽  
Stimulating Hormone

SUMMARY The distribution, potency and yield of growth hormone (GH), prolactin, thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH) and luteinizing hormone (LH) activities and the electrophoretic behaviour on starch gel have been studied in fractions obtained by chromatography on DEAE-cellulose of pituitary extracts from man, sheep, ox, pig and whale. In none of the species examined was the distribution of hormonal activities identical. GH, TSH and FSH in the sheep and ox, and GH and LH in the pig and whale, appeared in corresponding fractions. The prolactin activities from the five species were found in closely similar elution volumes. The hormonal activities of the human extract occurred over a much smaller range of distribution volumes than those of the other species. The GH fractions from all five species and the prolactins from sheep and ox were relatively potent preparations. Starch gel electrophoresis showed a number of components in all fractions. The distribution of components in corresponding fractions was different for each species, although some components had similar mobilities. These results add to the growing evidence of the species-specific nature of pituitary hormones and to the information available for evolving comprehensive fractionation systems for each species.

scholarly journals Biosynthesis of growth hormone in the rat anterior pituitary gland. Stimulation of biosynthesis in vitro by insulin

1973 ◽  
Vol 134 (4) ◽  
pp. 1103-1113 ◽  
Author(s):  
A. Betteridge ◽  
M. Wallis
Keyword(s):  
Growth Hormone ◽  
Anterior Pituitary ◽  
Rna Synthesis ◽  
Glucose Utilization ◽  
Actinomycin D ◽  
Hormone Synthesis ◽  
Pituitary Glands ◽  
Hormone Biosynthesis ◽  
Stimulation Of

The effect of insulin on the incorporation of radioactive leucine into growth hormone was investigated by using rat anterior pituitary glands incubated in vitro. A 50% stimulation over control values was observed at insulin concentrations above 2μm (280munits/ml). The effect was specific for growth hormone biosynthesis, over the range 1–5μm-insulin (140–700munits/ml). Lower more physiological concentrations had no significant effect in this system. Above 10μm (1.4 units/ml) total protein synthesis was also increased. The stimulation of growth hormone synthesis could be partially blocked by the addition of actinomycin D, suggesting that RNA synthesis was involved. Insulin was found to stimulate the rate of glucose utilization in a similar way to growth hormone synthesis. 2-Deoxyglucose and phloridzin, which both prevented insulin from stimulating glucose utilization, also prevented the effect of insulin on growth hormone synthesis. If glucose was replaced by fructose in the medium, the effect of insulin on growth hormone synthesis was decreased. We conclude that the rate of utilization of glucose may be an important step in mediating the effect of insulin on growth hormone synthesis.

Posttranscriptional regulation of rat growth hormone gene expression: increased message stability and nuclear polyadenylation accompany thyroid hormone depletion

1992 ◽  
Vol 12 (6) ◽  
pp. 2624-2632
Author(s):  
D Murphy ◽  
K Pardy ◽  
V Seah ◽  
D Carter
Keyword(s):  
Growth Hormone ◽  
Thyroid Hormone ◽  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Posttranscriptional Regulation ◽  
Anterior Pituitary Gland ◽  
Growth Hormone Gene ◽  
Gh Gene ◽  
Rat Growth ◽  
Pituitary Glands

In thyroid hormone-depleted rats, the rate of transcription of the growth hormone (GH) gene in the anterior pituitary gland is lower than the rate in euthyroid controls, and there is a corresponding reduction in the abundance of the GH mRNA. Concomitantly, the poly(A) tail of the GH mRNA increases in length. Examination of nuclear RNA from anterior pituitary glands of control and thyroid hormone-depleted rats revealed no difference in the length of pre-mRNAs containing the first and last introns of the GH gene. However, mature nuclear GH RNA is differentially polyadenylated in euthyroid and hypothyroid animals. We suggest that the extent of polyadenylation of the GH transcript is regulated in the cell nucleus concomitant with or subsequent to the splicing of the pre-mRNA. Experiments with anterior pituitary gland explant cultures demonstrated that the GH mRNA from thyroid hormone-depleted rats is more stable than its euthyroid counterpart and that the poly(A) tail may contribute to the differential stability of free GH ribonucleoproteins.

PREPARATION OF HUMAN GROWTH HORMONE

1961 ◽  
Vol 23 (3) ◽  
pp. 285-NP ◽  
Author(s):  
A. L. C. WALLACE ◽  
K. A. FERGUSON
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
High Yield ◽  
Pituitary Hormone ◽  
Simple Method ◽  
Anterior Pituitary Hormone ◽  
Epiphysial Cartilage ◽  
Diethylaminoethyl Cellulose ◽  
Hypophysectomized Rats

SUMMARY A simple method for the preparation of human growth hormone using chromatography on diethylaminoethyl-cellulose is described. Material prepared in this way, when assayed by growth of the tibial epiphysial cartilage in hypophysectomized rats, is at least as active as material prepared by published methods and is obtained in high yield. The only other anterior pituitary hormone activity present in any concentration is prolactin.

Sign in / Sign up

Export Citation Format

Share Document