IMMUNOLOGICAL ESTIMATION OF SHEEP GROWTH HORMONE

1962 ◽  
Vol 24 (2) ◽  
pp. 171-178 ◽  
Author(s):  
A. L. C. WALLACE
Keyword(s):  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Haemagglutination Inhibition ◽  
Homogeneous Component ◽  
Biological Assay ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Assay Methods ◽  
Inhibition Reaction ◽  
Good Agreement

SUMMARY An electrophoretically homogeneous component obtained by starch gel electrophoresis of sheep growth hormone (GH) has been used to prepare antiserum in rabbits. By means of a haemagglutination—inhibition reaction, this antiserum was used to assay GH both in sheep pituitary extracts and in sheep sera. The values for the GH content of a number of pituitary extracts obtained by both immunological and biological assay methods were in good agreement. GH levels in sheep serum were found to range between 38 and 600 μg./100 ml.

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.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

STUDIES ON HUMAN CHORIONIC GONADOTROPHIN

1968 ◽  
Vol 59 (1) ◽  
pp. 120-138 ◽  
Author(s):  
A. H. W. M. Schuurs ◽  
E. de Jager ◽  
J. D. H. Homan
Keyword(s):  
Gel Electrophoresis ◽  
Complement Fixation ◽  
Haemagglutination Inhibition ◽  
Fundamental Difference ◽  
Chorionic Gonadotrophin ◽  
Human Chorionic Gonadotrophin ◽  
Starch Gel Electrophoresis ◽  
International Standard ◽  
Electrophoretic Mobilities ◽  
Starch Gel

ABSTRACT Preparations of Human Chorionic Gonadotrophin (HCG) with varying degrees of homogeneity were investigated immunochemically. The preparations were compared qualitatively by combined starch gel electrophoresis and immunoelectrophoresis, by immunodiffusion and immunoelectrophoresis in agar, and, quantitatively by haemagglutination inhibition and by complement fixation reactions. The components present in pure HCG preparations which differed in electrophoretic mobilities, in N-acetyl neuraminic acid (NANA) content and in biological potencies, appeared to be immunochemically identical. This implies that results of immunochemical and biological estimations need not correlate with each other. This finding is compared with relevant data in the literature. It is proposed to use the 2nd International Standard for HCG for both immunochemical and biological estimations, but, because of the fundamental difference between the results of the two types of estimations, to express the immunochemically determined values in »International Immunochemical Units« (IIU).

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.

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.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

Sign in / Sign up

Export Citation Format

Share Document