Starch gel electrophoresis of extracts of human anterior pituitary glands and tumours

1965 ◽  
Vol 11 (3) ◽  
pp. 238-243 ◽  
Author(s):  
H.M. Lloyd ◽  
J.D. Meares
Keyword(s):  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Starch Gel Electrophoresis ◽  
Pituitary Glands ◽  
Starch Gel ◽  
Human Anterior Pituitary

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.

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.

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.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

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