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.

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.

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.

DISTRIBUTION OF SOLUBLE PROTEINS IN THE MAMMALIAN NEUROHYPOPHYSIS AND THEIR CROSS-SPECIES REACTIVITY WITH ANTI-NEUROPHYSIN

1972 ◽  
Vol 55 (3) ◽  
pp. 565-575 ◽  
Author(s):  
H. K. ELLIS ◽  
W. B. WATKINS ◽  
J. J. EVANS
Keyword(s):  
Mammalian Species ◽  
Fallow Deer ◽  
Soluble Proteins ◽  
Starch Gel Electrophoresis ◽  
Osmotic Stimulation ◽  
Pituitary Glands ◽  
Starch Gel ◽  
Stimulation Experiments ◽  
Neurophysin Ii ◽  
Selection Of

SUMMARY Pituitary glands were collected from a selection of 22 domestic and exotic mammalian species. The soluble proteins extracted from the neurohypophyses were characterized by horizontal starch-gel electrophoresis at pH 8·1. Those species which were closely related phylogenetically, e.g. fallow deer and muntjac deer, pig and hippopotamus, dog and coatimundi, and members of the primates, had similar and in some cases identical protein profiles. The ability of proteins extracted from the starch-gel to cross-react immunologically with an antiserum raised against porcine neurophysin-II was determined by microimmunodiffusion. Using this technique for the identification of neurophysins in conjunction with osmotic stimulation experiments, it was found that the number of major neurophysins present in the mammalian neurohypophyses studied varied from one in the guinea-pig and hedgehog to four in man. The concept of multiple neurophysins is discussed.

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.

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.

Bovine Platelet Proteins II. Purification of Platelet Fibrinogen

1969 ◽  
Vol 21 (03) ◽  
pp. 419-427 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk
Keyword(s):  
Analytical Ultracentrifugation ◽  
Insoluble Fraction ◽  
Disc Electrophoresis ◽  
Plasma Fibrinogen ◽  
Starch Gel Electrophoresis ◽  
Freezing And Thawing ◽  
Insoluble Material ◽  
High Resolution Power ◽  
Starch Gel ◽  
Platelet Proteins

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.

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.

Experimental Measurement of In-Plane Rolling Nonpneumatic Tire Vibrations Using High-Speed Imaging

2019 ◽  
Vol 47 (3) ◽  
pp. 196-210
Author(s):  
Meghashyam Panyam ◽  
Beshah Ayalew ◽  
Timothy Rhyne ◽  
Steve Cron ◽  
John Adcox
Keyword(s):  
High Speed ◽  
Image Correlation ◽  
Dynamic Mode Decomposition ◽  
Dynamic Mode ◽  
High Speed Imaging ◽  
Correlation Algorithm ◽  
Mode Decomposition ◽  
Series Of Experiments ◽  
Plane Deformations ◽  
Dominant Frequencies

ABSTRACT This article presents a novel experimental technique for measuring in-plane deformations and vibration modes of a rotating nonpneumatic tire subjected to obstacle impacts. The tire was mounted on a modified quarter-car test rig, which was built around one of the drums of a 500-horse power chassis dynamometer at Clemson University's International Center for Automotive Research. A series of experiments were conducted using a high-speed camera to capture the event of the rotating tire coming into contact with a cleat attached to the surface of the drum. The resulting video was processed using a two-dimensional digital image correlation algorithm to obtain in-plane radial and tangential deformation fields of the tire. The dynamic mode decomposition algorithm was implemented on the deformation fields to extract the dominant frequencies that were excited in the tire upon contact with the cleat. It was observed that the deformations and the modal frequencies estimated using this method were within a reasonable range of expected values. In general, the results indicate that the method used in this study can be a useful tool in measuring in-plane deformations of rolling tires without the need for additional sensors and wiring.

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