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.

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.

A STUDY OF PROLACTIN-LIKE ACTIVITY IN INDIVIDUAL HUMAN PITUITARY GLANDS

1970 ◽  
Vol 48 (4) ◽  
pp. 639-647 ◽  
Author(s):  
PATRICIA M. NICHOLSON
Keyword(s):  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Post Partum ◽  
Human Pituitary ◽  
Lactating Women ◽  
Pituitary Glands ◽  
Human Anterior Pituitary ◽  
Pituitary Prolactin ◽  
Individual Human

SUMMARY Polyacrylamide disc gel electrophoresis of aqueous extracts of individual human anterior pituitary glands failed to identify a protein with lactogenic activity which was characteristic of pregnancy and the post-partum period. Lactogenic activity, determined by a semi-quantitative rabbit mammary gland organ culture assay, was largely associated with the growth hormone fraction. The total prolactin activity of individual anterior pituitary glands was determined by a 'local' intradermal pigeon crop sac method. The glands from pregnant and parturient women did not contain a higher concentration of prolactin than those of men or non-pregnant non-lactating women. These results do not provide any evidence for the existence of a human pituitary prolactin distinct from growth hormone. Reasons for this are discussed.

STARCH-GEL ELECTROPHORESIS OF MOUSE PITUITARY GONADOTROPHINS

1968 ◽  
Vol 40 (3) ◽  
pp. 313-323 ◽  
Author(s):  
H. M. LLOYD ◽  
B. M. BINDON ◽  
D. R. LAMOND ◽  
J. D. MEARES
Keyword(s):  
High Speed ◽  
Light Exposure ◽  
Follicle Stimulating Hormone ◽  
Active Material ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Method ◽  
Pituitary Glands ◽  
Starch Gel ◽  
Series Of Experiments ◽  
Mouse Pituitary

SUMMARY Extracts of mouse pituitary glands, prepared by homogenization and high-speed centrifugation, were separated into 16–17 fractions by preparative electrophoresis in starch gel, from which the proteins were then recovered by an electrophoretic method. Follicle-stimulating hormone (FSH), assayed by the uterine-weight augmentation method in the hypophysectomized mouse, was confined to 2–3 adjacent portions of the gel 1 cm. wide. Luteinizing hormone (LH) assayed by the rat ovarian ascorbic-acid depletion method was recovered from three discrete regions of the gel, well separated from FSH. The most active LH fraction was of slower mobility than the FSH. Assay for 'total' gonadotrophin, using normal mouse uterine weights, disclosed active material of slow mobility, separated from the FSH fractions. A series of experiments devoted to assays of FSH separated electrophoretically from pooled mouse pituitary glands demonstrated variations in pituitary content and concentration of FSH related to sex, age, pregnancy, lactation, dietary changes and light exposure which were consistent with results of previous studies of the mouse and of the rat.

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.

BIOLOGICAL AND IMMUNOLOGICAL PROPERTIES OF HUMAN PITUITARY FOLLICLE STIMULATING HORMONE OBTAINED BY STARCH GEL ELECTROPHORESIS

1963 ◽  
Vol 25 (4) ◽  
pp. 541-547 ◽  
Author(s):  
W. R. BUTT ◽  
A. C. CROOKE ◽  
F. J. CUNNINGHAM ◽  
ANNELIESE WOLF
Keyword(s):  
Follicle Stimulating Hormone ◽  
Haemagglutination Inhibition ◽  
Chorionic Gonadotrophin ◽  
Starch Gel Electrophoresis ◽  
Minimum Effective Dose ◽  
Hormone Activity ◽  
Human Pituitary ◽  
Main Fraction ◽  
Starch Gel ◽  
Stimulating Hormone

SUMMARY A highly potent preparation of human follicle stimulating hormone (FSH) was submitted to electrophoresis in starch gel. A fraction containing luteinizing hormone activity was separated from the main fraction of FSH. The latter showed no luteinizing activity by the ovarian ascorbic acid depletion method with 125 times the minimum effective dose in the assay for FSH. Synergistic joint action (see p. 544) was shown between the two fractions. An antiserum raised to the follicle stimulating component was investigated by red cell haemagglutination-inhibition tests. Its titre was only slightly reduced after absorption with chorionic gonadotrophin and haemagglutination was inhibited by preparations of FSH containing 0·5 μg./ml. (1·5 mg. HMG 24/ml.), but not by solutions of chorionic gonadotrophin containing up to 100 i.u./ml. This is regarded as evidence that the antiserum is fairly specific for FSH.

ELECTROPHORESIS IN STARCH GEL OF EXTRACTS OF HUMAN ANTERIOR PITUITARY GLANDS, WITH BIOASSAY OF GONADOTROPHIN

1962 ◽  
Vol 39 (2) ◽  
pp. 163-174 ◽  
Author(s):  
H. M. Lloyd ◽  
J. D. Meares
Keyword(s):  
Anterior Pituitary ◽  
High Speed ◽  
Serum Proteins ◽  
Preparative Method ◽  
Variable Number ◽  
Mouse Uterus ◽  
Pituitary Glands ◽  
Starch Gel ◽  
Human Anterior Pituitary ◽  
Supernatant Solution

ABSTRACT Extracts of human anterior pituitary glands were prepared by homogenization and high speed centrifugation. The particle-free supernatant solution were subjected to electrophoresis on paper, in starch grain and in starch gel. A preparative method for electrophoresis in starch gel was devised. Separation of serum proteins into 14 zones was obtained with this method and the patterns obtained with pituitary extracts showed three major zones, one of which was haemoglobin, and a variable number of other zones. Protein recovered after electrophoresis from portions of the gel was tested for gonadotrophin by the mouse uterus test. Gonadotrophic activity was found among the more slowly moving fractions and could not be correlated with any individual protein zones revealed by staining with nigrosine.

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