scholarly journals The induction of cross-links in soluble rat skin collagen in vitro

1969 ◽  
Vol 114 (3) ◽  
pp. 509-512 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Gel Electrophoresis ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Skin Collagen ◽  
Cross Linkage ◽  
Starch Gel ◽  
Cross Links

1. Starch-gel electrophoresis was used to investigate the subunit composition of salt-soluble and acid-soluble rat skin collagen. 2. Cross-linkage of collagen subunits in vitro was performed (a) when in fibrillar form and (b) when in solution. In the former case the increase in number of cross-links appeared to be predominantly intermolecular and in the latter case predominantly intramolecular.

scholarly journals The relationship between reversibility of fibril formation and subunit composition of rat skin collagen

1969 ◽  
Vol 113 (2) ◽  
pp. 419-422 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Fibril Formation ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Fractionation Procedure ◽  
Skin Collagen ◽  
Starch Gel ◽  
The Relationship

1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37°. On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.

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.

Enzymatic Modifications of the Protamines. II. Separation and Characterization of Phosphorylated Species of Protamines from Trout Testis

1974 ◽  
Vol 52 (6) ◽  
pp. 536-546 ◽  
Author(s):  
Andrew J. Louie ◽  
Gordon H. Dixon
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Stage Of Development ◽  
Phosphorylated Amino Acid ◽  
Similar Series ◽  
Starch Gel ◽  
Derivatives Of

Substantial quantities of highly phosphorylated protamines were prepared from hormonally induced trout testes at the early protamine stage of development. Purified protamines from testes induced to mature by injection of salmon pituitary extracts were resolved into eight fractions on long carboxymethyl cellulose columns by eluting with a gradient of LiCl in the presence of 6 M urea; only two major fractions were found in protamine extracted from naturally maturing testes. Each fraction was not homogenous but consisted of a mixture of several related protamines. Analysis of radioactivity in in vivo32P-labeled protamine indicated that six of the eight fractions were phosphorylated. Amino acid analysis, phosphate determinations, and starch gel electrophoresis indicated that three of the phosphorylated peaks correspond to the mono-, di-, and triphosphorylated derivatives of the first fraction (three serines) of protamine, while the other three correspond to a similar series of the second fraction (four serines) of protamine. These protamines with differing levels of phosphorylation may be useful for in vitro studies of the interaction of phosphoprotamines with DNA or chromatin.

scholarly journals Production of Dihaploids in Carnation (Dianthus caryophyllus L.)

HortScience ◽  
1997 ◽  
Vol 32 (3) ◽  
pp. 461A-461
Author(s):  
Ramon Dolcet-Sanjuan ◽  
Elisabet Clavería ◽  
Alfonso J. Rodríguez ◽  
Marta Llaurado
Keyword(s):  
Gel Electrophoresis ◽  
Embryo Rescue ◽  
Dianthus Caryophyllus ◽  
Somatic Tissue ◽  
Starch Gel Electrophoresis ◽  
Regenerated Plants ◽  
In Vitro Micropropagation ◽  
Starch Gel ◽  
Gamma Irradiated

Callus and shoot organogenesis were obtained from anthers of Dianthus caryophyllus L. `Manon', `Amapola', `Elsy', and `IB212', harboring mid-uninucleated microspores. Significant differences between genotypes were observed on number of responsive anthers (10.4% to 72.1%) and rescued plants per responsive anthers (1.2% to 4.8%). A modified H medium (Nitsch and Nitsch, 1969) with 20 g/L maltose and 0.25% Gelrite, supplemented with 10 μM 2,4-D and 1 μM TDZ, was most appropriate for callus induction. Plants were regenerated after subsequent subculture to the same medium, but amended with 0.1 μM TDZ. Zymogram types for aminopeptidase (AAP) in polyacrilamide gel electrophoresis proved that all 40 plants regenerated from `Amapola', `Elsy', or `IB212' where heterozygous, and consequently not originated from the microspores but from somatic tissue. Alternatively, in situ-induced parthenogenesis through pollination with gamma-irradiated pollen and in vitro embryo rescue was tested. A total of 92 embryos, including normal and no cotyledonary embryos, were rescued from 38 fruits harvested out of 70 crosses between `Scania' and `Amapola'. Embryos were rescued 21 to 28 days after pollination by culture in a modified E20A (Sauton and Vaulx, 1987) medium. Phosphogluco isomerase (PGI) and Shikimic dehydrogenase (SDH) zymograms in starch gel electrophoresis, and AAP in polyacrilamide gel electrophoresis, indicated the parthenogenic origin of three of the regenerated plants. Flow cytometry of nuclei proved the early diploidization, during in-vitro micropropagation, of the parthenogenic carnation haploid plantlets.

A Study of Detergent Pollution By Molecular Methods: Starch Gel Electrophoresis of a Variety of Enzymes and Other Proteins

1967 ◽  
Vol 47 (3) ◽  
pp. 659-675 ◽  
Author(s):  
Clyde Manwell ◽  
C. M. Ann Baker
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Marine Species ◽  
Serum Lipoprotein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Irreversible Effect ◽  
General Opinion

Tissues from a number of marine species were treated with a variety of solutions, including 1% of the major ‘detergent’ (B.P. 1002) used in attempting to disperse the oil from the ‘Torrey Canyon’ and 1% of each of the three major constituents of B.P. 1002, two of which are non-ionic surfactants.The extracts were submitted to vertical starch-gel electrophoresis in order to measure both the effect of the detergent in facilitating the breakdown of cellular structure (extractability), and the irreversible effect on activation or inhibition of various enzymes and other proteins.The proteins studied include a variety of NAD- and NADP-linked dehydrogenases, esterases, blood and nerve haemoglobins, plasma proteins, egg white and yolk proteins, and r-phycoerythrin.The results confirm the general opinion that detergents increase the extractability of proteins from cells. In particular lipoprotein systems are altered, e.g. ‘fast’ serum lipoprotein in fishes (and other vertebrates). Other effects are also observed, e.g. sole but not turbot haemoglobin is rendered relatively insoluble, probably because the detergent stabilizes haemoglobin binding to other components in the erythrocyte. Certain enzymes, e.g. some esterases and amylases, are activated—a not surprising observation. However, a few enzymes are altered in electrophoretic mobility or in activity in a way that one might not expect, e.g. bass Morone labrax lactate dehydrogenase.The results indicate that ‘oil-spill’ detergents and their constituent surfactants are biochemically quite powerful agents. It is too early to attempt to correlate in vitro and in vivo observations but there is an indication that starch-gel electrophoresis provides a useful supplement to more conventional methods used in the studies on complex pollution problems.

scholarly journals A new subunit of horse liver alcohol dehydrogenase and subunit composition of the polymorphic form

1976 ◽  
Vol 153 (2) ◽  
pp. 249-257 ◽  
Author(s):  
R Pietruszko ◽  
C N Ryzewski
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Electrophoresis ◽  
Catalytic Properties ◽  
Polymorphic Form ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Starch Gel

The most cathodal (on starch-gel electrophoresis), steroid-active band of horse liver alcohol dehydrogenase, whose catalytic properties were shown to be dependent on the livers used as a starting material [Pietruszko (1974) Biochem. Biophys. Res. Commun. 60, 687-694], has been prepared from A-type and S-type horse livers by identical methods. Results presented here show that different isoenzymes are present in these preparations.

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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