PURIFICATION AND PROPERTIES OF THE FOLLICLE-STIMULATING HORMONE INHIBITOR OBTAINED FROM THE URINE OF THE BONNET MONKEY

1968 ◽  
Vol 40 (2) ◽  
pp. 165-173 ◽  
Author(s):  
M. R. SAIRAM ◽  
H. G. MADHWA RAJ ◽  
N. R. MOUDGAL

SUMMARY The follicle-stimulating hormone (FSH) inhibitor in monkey urine was purified by selective extraction of the crude extract with acetate buffer, ammonium sulphate precipitation and DEAE-cellulose chromatography. The purified inhibitor was free of luteinizing hormone activity. It behaved as an apparently homogeneous protein. The inhibitor contained about 20% carbohydrate (hexoses, hexosamines, fucose and sialic acid). Thin-layer gel filtration indicated a molecular weight of about 65,000. The inhibitor was labile to heat treatment, exposure to extremes of pH and denaturing agents. The inhibitor effectively neutralized the biological activity of FSH preparations from human, monkey, horse, pig, sheep and rat pituitary glands, pregnant mare serum gonadotrophin and human pituitary urinary gonadotrophin.

1972 ◽  
Vol 71 (3) ◽  
pp. 443-453 ◽  
Author(s):  
Olav Trygstad ◽  
Irene Foss

ABSTRACT A lipid-mobilizing factor (LMF) with an adipotrophic effect in human and animal fat tissue has been prepared from human pituitary glands. The addition of normal human serum to LMF reduced its lipolytic effect, and it was completely abolished by serum from a group of obese patients, whereas the lipolysis was not influenced by serum from patients with generalized lipodystrophy. By DEAE-cellulose chromatography of human serum the inhibitory effect on LMF was found to be present in a protein fraction less acidic than the main serum albumin fraction. The inhibitory fraction was deprived of some contaminants by Sephadex gel filtration. Disc electrophoresis demonstrated the presence of three components in the inhibitory protein (IP), and they were identified as albumin, transferin, and haemopexin by immuno-electrophoresis. Precipitation of these proteins by their rabbit antisera demonstrated that the inhibitory effect was present in the albumin fraction. Insulin like activity was not observed in IP. A protein binding of LMF by IP could not be demonstrated. Incubation at 37°C for one hour of a mixture of LMF and IP eliminated the electrophoretic picture of LMF. It is concluded that the inhibitory effect of human serum may be due to proteolysis of LMF.


1969 ◽  
Vol 7 (9) ◽  
pp. 33-35

The three substances now used to stimulate the gonads in infertility are human follicle stimulating hormone (HFSH) obtained mainly from post-menopausal urine, but also from human pituitary glands, human chorionic gonadotrophin (HCG) extracted from the urine of pregnant women, and clomiphene (Clomid - Merrell), a synthetic compound which we reviewed in 1967.1


1968 ◽  
Vol 57 (2) ◽  
pp. 289-295 ◽  
Author(s):  
E. Steinberger ◽  
G. Duckett

ABSTRACT On the basis of a study of changes in follicle stimulating hormone (FSH) levels in rat pituitary glands, obtained at various times after orchiectomy, it has been previously suggested that the Leydig cell secretions may regulate the release of FSH from the pituitary gland (Steinberger & Duckett 1966). This hypothesis was put to test in the present study. FSH levels have been determined in the pituitary gland and plasma of normal, testosterone-treated, orchiectomized, and orchiectomized testosteronetreated rats. A marked drop of pituitary FSH levels, associated with an elevation of plasma FSH levels, was observed in orchiectomized rats. Administration of testosterone to orchiectomized rats prevented the drop in pituitary FSH levels and rendered the blood levels undetectable. These results are interpreted as supporting the hypothesis that testosterone has an inhibitory effect on the release of FSH from the pituitary gland.


1976 ◽  
Vol 159 (3) ◽  
pp. 651-659 ◽  
Author(s):  
K W Cheng

A reproducible procedure was developed for the purification of follitropin from frozen bovine pituitary glands. The method involved precipitation with (NH4)2SO4 and acetone, followed by ion-exchange column chromatography on CM-cellulose and DEAE-cellulose and gel filtration on Sephadex G-100. A specific radioligand-receptor assay for follitropin was used to locate the activity in eluates after column chromatography and gel filtration. The potency of the highly purified bovine follitropin as measured by Steelman-Pohley bioassay was 164 times that of NIH-FSH-S1 standard preparation. They yield of bovine follitropin was 2.9 mg/kg of frozen pituitary glands. Electrophoretically, bovine follitropin was more acidic in nature and migrated further towards the anode than lutropin and thyrotropin. The elution volume of bovine follitropin by gel filtration on Sephadex G-100 was very similar to that of bovine lutropin. The amino acid composition of bovine follitropin was similar to that of sheep and human follitropin, being rich in lysine, aspartic acid, threonine, serine, glutamic acid and half-cystine.


1969 ◽  
Vol 43 (4) ◽  
pp. 609-616 ◽  
Author(s):  
ANNE STOCKELL HARTREE ◽  
F. J. CUNNINGHAM

SUMMARY Separation and partial purification of chicken pituitary follicle-stimulating hormone (FSH) and luteinizing hormone (LH) has been obtained by methods which were effective in the purification of the corresponding human and horse hormones. Increases in chicken LH activity were observed after chromatography on DEAE-cellulose and on Amberlite IRC-50 suggesting removal of an LH inhibitor. The biological potencies of chicken FSH and LH preparations when assayed in mammals were very much lower than those of the corresponding mammalian fractions on a weight basis. A weak immunological cross-reaction between chicken and human pituitary LH was used to estimate LH in chicken pituitary fractions and the results were compared with bioassays of the same fractions.


1962 ◽  
Vol 24 (2) ◽  
pp. 223-225 ◽  
Author(s):  
W. R. BUTT ◽  
A. C. CROOKE ◽  
F. J. CUNNINGHAM ◽  
NADA KOVAČIĆ

SUMMARY Four gonadotrophic fractions from human pituitary glands have been assayed in terms of the International Reference Preparation, HMG 24, by four different methods. These are the assay for total gonadotrophin which depends on the increase in uterine weight of the immature mouse, the augmentation method for follicle-stimulating hormone, the increase in weight of the ventral prostate of the hypophysectomized rat for interstitial cell-stimulating hormone and the ovulation method for the 'ovulating ' factor. The results have been contrasted and discussed.


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