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 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 Starch-Gel Electrophoresis of Wheat Flour Proteins

1963 ◽  
Vol 16 (2) ◽  
pp. 342 ◽  
Author(s):  
Janet SD Graham
Keyword(s):  
Acetic Acid ◽  
Wheat Flour ◽  
Gel Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Similar Protein ◽  
Starch Gel ◽  
Protein Components ◽  
Electrophoresis Of Proteins

An improved apparatus and procedures for starch-gel electrophoresis of proteins of wheat flour are described; highly reproducible separation of the protein components was achieved. By starch-gel electrophoresis it was shown that similar protein components occur in the extracts of wheat flour obtained with a variety of solvents; however, there were marked differences in the proportions of these components in various extracts. Several protein components were present in the fJ'actions separated by ion-exchange chromatography of' the proteins soluble in Bodium pyrophosphate and of those soluble in acetic acid; some fractions containeda number of similar protein components.

The relationship between nematodes of the genus Cosmocercoides Wilkie, 1930 (Nematoda: Cosmocercoidea) in toads (Bufo americanus) and slugs (Deroceras laeve)

1987 ◽  
Vol 65 (7) ◽  
pp. 1650-1661 ◽  
Author(s):  
Daryl J. Vanderburgh ◽  
R. C. Anderson
Keyword(s):  
Discriminant Analysis ◽  
Gel Electrophoresis ◽  
Analysis Of Covariance ◽  
Starch Gel Electrophoresis ◽  
Bufo Americanus ◽  
Cross Transmission ◽  
Starch Gel ◽  
The Relationship

Nematodes of the genus Cosmocercoides Wilkie, 1930 from Bufo americanus and Deroceras laeve, generally considered to belong to the same species (Cosmocercoides dukae), were compared. Male worms from B. americanus had 20 or 21 rosette papillae per subventral row whereas males from D. laeve had 13 to 14. Worms from toads had numerous simple postanal papillae. Worms from slugs generally lacked such papillae. Worms from the two hosts differed morphometrically and were well separated by discriminant analysis after bias of worm length was removed by analysis of covariance. Differences in isoenzyme migration were detected using starch gel electrophoresis. In cross-transmission experiments, more toads became infected when exposed to larvae of worms from toads than when exposed to larvae of worms from slugs. More slugs became infected when exposed to larvae from slugs than when exposed to larvae from toads. Intensity of mature worms recovered was significantly (p < 0.05) greater (and patent infections developed) when transmission was from toad to toad or from slug to slug than when transmission was from toad to slug or from slug to toad. No patent infections were recorded from toads or slugs exposed to larvae from the unrelated host. The results indicate that worms in toads and slugs are not conspecific. Cosmocercoides variabilis (Harwood, 1930) Travassos, 1931 is resurrected as the name of the species occurring in B. americanus, Cosmoceroides dukae (Holl, 1928) Travassos, 1931 is retained as the name of the species occurring in D. laeve.

Hemoglobin Mahidol: a new hemoglobin α-chain mutant

1970 ◽  
Vol 48 (9) ◽  
pp. 1066-1078 ◽  
Author(s):  
S. Pootrakul ◽  
G. H. Dixon
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Cyanogen Bromide ◽  
Starch Gel Electrophoresis ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Α Chain ◽  
Acid Alteration ◽  
Peptide Maps ◽  
Amino Acid Alteration

A slow (less anionic) hemoglobin mutant has been detected by starch gel electrophoresis of hemoglobin from three unrelated patients in Bangkok. Dissociation of the abnormal hemoglobin with p-hydroxymercuribenzoate showed that the α-chain was the site of the mutation. The mutant α-chain was isolated by carboxymethylcellulose chromatography in 8 M urea and 0.05 M β-mercaptoethanol. Peptide maps of trypsin and cyanogen bromide cleaved α-chain indicated that the amino acid alteration of the mutant was in the peptide corresponding to residues 62–76 of the α-chain. Further cleavage of this peptide with 0.25 M acetic acid at 110 °C showed that residue 74 was changed from an aspartyl to a histidyl residue, a mutation not previously described. It is proposed that this new hemoglobin α274His β2A be called hemoglobin Mahidol after Mahidol University in Bangkok. In one of the three patients showing hemoglobin Mahidol, interaction with α-thalassemia occurs and, in this patient, hemoglobin A is totally absent, being replaced by hemoglobin Mahidol together with some hemoglobin H (β4A).

scholarly journals The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart

1974 ◽  
Vol 141 (2) ◽  
pp. 401-406 ◽  
Author(s):  
Robert John ◽  
Richard Jones
Keyword(s):  
Aspartate Aminotransferase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Wide Range ◽  
Covalent Structure ◽  
Starch Gel ◽  
The Difference ◽  
Ph Range ◽  
The Relationship ◽  
Charged Group

Starch-gel electrophoresis of sheep heart aspartate aminotransferase was carried out over the range pH7.0–8.5. The enzyme separates into three subforms in the same way as the pig heart enzyme. As the pH was increased the distance migrated by each subform increased by the same amount, so that they remained the same distance apart. Titration of the enzyme over the appropriate pH range was used to calculate the difference in charge between the subforms and it was concluded that they differ by one charged group per dimer from their nearest neighbour on the electrophoretogram over the whole pH range studied. It was also shown that the pig-heart α and β subforms differ by almost one charged group per dimer in the range pH5.5–5.7 and that the spacing between the subforms on starch-gel electrophoresis at pH8.0 is the same as that for the sheep enzyme. Since the charge difference between the subforms is maintained over such a wide range of pH, it is concluded that they probably differ from each other in covalent structure, because of the improbability that conformational differences can give rise to such behaviour. The relationship between the subforms and inactive binding of the coenzyme is also examined.

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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