A Microelectrophoretic and Microionophoretic Technique<sup>1</sup>

Durrum, E. L.

doi:10.1021/ja01163a037

Cited by 445 publications

(106 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The apparatus used was similar to that described by Durrum (13). t Three inch wide strips of Whatmaun 3 MM paper were run for 4 hours at room temperature in veronal buffer (pH 8.6, ~ --0.10) at an initial current of 4 to 5 milliamperes.…”

Section: Paper Electrophoresismentioning

confidence: 99%

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

Slade¹,

Slamp²

1955

The Journal of Experimental Medicine

View full text Add to dashboard Cite

Crystalline ovalbumin, when heated under controlled conditions, promoted growth of Streptococcus hemolyticus in a synthetic medium. A similar activation of albumin also was produced by ultraviolet irradiation or by shaking under nitrogen. Untreated albumin failed to permit growth under the same conditions. The activity of treated albumin was destroyed by aeration or by reaction with iodoacetate. The data suggest that the activity of ovalbumin for the streptococcus depends on the presence of "exposed" SH groups. However, other sulfhydryl-containing compounds (thioglycolate, glutathione, cysteine) could not replace ovalbumin. A number of crude and crystalline proteins, and di- and tripeptides were inactive. Strepogenin and crystalline bovine serum albumin produced a weak growth response on extended incubation. Approximately 50 per cent of the original protein in the culture disappeared during growth. Ovalbumin labelled with C14 was added to the synthetic medium. After growth of the culture the isotope was found associated with the cells and in the culture fluid in both dialyzable and non-dialyzable forms. Under the conditions described, luxuriant growth of 15 strains (10 serological types) of Group A streptococci was obtained in 10 hours from small inocula. The growth was capable of repeated subcultivation.

show abstract

Section: Paper Electrophoresismentioning

confidence: 99%

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

Slade¹,

Slamp²

1955

The Journal of Experimental Medicine

View full text Add to dashboard Cite

show abstract

“…Paper electrophoretic analyses were carried out in a Durrum cell (12) with barbital buffer of pH 8.6, ionic strength 0.05. Bromphenol blue was used for protein staining and Sudan black for lipid staining.…”

mentioning

confidence: 99%

FURTHER CHARACTERIZATION OF THE HUMAN SERUM D 1.063-1.21, Α1-Lipoprotein*

Scanu¹,

Hughes²

1962

J. Clin. Invest.

View full text Add to dashboard Cite

The high density lipoprotein class floating at a solvent density between 1.063 and 1.21 g per ml can be fractionated by flotation in solvents of intermediate density into two major subfractions (1, 2), which according to Shore (3) have a protein moiety with identical amino acid composition and C-and N-terminal amino acids. Homogeneity of the D 1.063-1.21 lipoprotein in terms of protein moiety has also been indicated by immunochemical studies (4). It would appear, therefore, that the human serum high density lipoprotein of D 1.063-1.21 constitutes a group of molecules identical as to protein moiety and possibly differing only in lipid complement. The experiments reported below were designed to test this hypothesis. The serum D 1.063-1.21 lipoprotein was arbitrarily fractionated into three fractions floating respectively at solvent densities of D 1.063-1.125, 1.125-1.168, and 1.168-1.21. The results dealing with some of the physicochemical and biological properties of these lipoprotein subfractions form the object of this report. MATERIAL AND METHODSThe source of the lipoproteins was pooled sera from healthy human male subjects, fasted for at least 12 hours.

show abstract

“…Woods and Gillespie (1953). The distribution of protein along the paper was determined by the dyeing procedure of Durrum (1950) and also by the less sensitive spectrophotometric measurement of water eluates at 278 m[l. Owing to differences in affinity of different proteins for dye and differences in the absorption of radiation at 278 m[l, neither method provides an absolute measure of protein distribution.…”

Section: ( B) Protein Estimationmentioning

confidence: 99%

“…INTRODUCTION Cohn et al (1946, 1950 have developed the basic procedures for separating plasma proteins by ethanol fractionation at low temperatures and low ionic strengths and their methods have been used for enzyme fractionation by Ellis and Fruton (1951) and Askonas (1951) and in the investigations described in the present paper .…”

mentioning

confidence: 97%

Enzymes of Aspergillus Oryzae V. Ethanol Fractionation at Low Ionic Strengths

Gillespie¹,

ood²

1953

Aust. Jnl. Of Bio. Sci.

View full text Add to dashboard Cite

SummaryMoving boundary and paper electrophoresis were applied to crude and deionized enzyme preparations from cultures of Aspergillus oryzae. Five main protein components were observed by both methods and four additional minor components were demonstrated with the paper method.After paper electrophoresis the main protein component was found to correspond with a protease and an esterase with isoelectric points at pH 5.1. A second protease less active than the other protease in digesting gelatin, with an isoelectric point of 4.2, and a second esterase of isoelectric point 3.9, were also characterized. Sucrase appeared as a single peak whereas amylase and cellulase showed at least six and seven peaks respectively.Solubility curves of dialysed crude mould enzyme in ethanol-water mixtures at low temperatures were atypical in that variation of pH and ionic strength had little effect on the solubility owing to the presence of 70 per cent. ionic material. Removal of this material with ion exchange resins also removed about 50 per cent. of the enzyme protein, whereas electrodialysis removed it almost completely without loss in enzyme activity. Material treated in this way was found to provide typical pH-solubility curves having well-defined solubility minima near the isoelectric point of the major protease (pH 5.1). Using this data two proteases were separated from each other 'and, after reprecipitation at the isoelectric point, the major protease was obtained electrophoretically pure.A crystalline preparation of mould protease was shown to contain a single component representing approximately 90 per cent. of the protein present and having mobility corresponding to that of the major protease.

show abstract

A Microelectrophoretic and Microionophoretic Technique¹

Cited by 445 publications

References 0 publications

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

FURTHER CHARACTERIZATION OF THE HUMAN SERUM D 1.063-1.21, Α1-Lipoprotein*

Enzymes of Aspergillus Oryzae V. Ethanol Fractionation at Low Ionic Strengths

Contact Info

Product

Resources

About

A Microelectrophoretic and Microionophoretic Technique1

Cited by 445 publications

References 0 publications

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

The Requirement of Ovalbumin for the Growth of Group a Hemolytic Streptococcus in a Synthetic Medium

FURTHER CHARACTERIZATION OF THE HUMAN SERUM D 1.063-1.21, Α1-Lipoprotein*

Enzymes of Aspergillus Oryzae V. Ethanol Fractionation at Low Ionic Strengths

Contact Info

Product

Resources

About

A Microelectrophoretic and Microionophoretic Technique¹