STARCH GEL ELECTROPHORESIS OF COBRA AND RATTLESNAKE VENOMS

1963 ◽  
Vol 41 (1) ◽  
pp. 1073-1078 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Sodium Acetate ◽  
Acetate Buffer ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Acetate Buffer ◽  
Cacodylate Buffer ◽  
Starch Gel ◽  
Acidic Proteins

The effect of pH on gradient starch gel electrophoresis of the venoms of Crotalus adamanteus and Naja flava has been examined. Sodium acetate buffer, pH 4.1, ionic strength 0.020, appeared most effective for resolution of the former venom, and acetate buffer, pH 4.7, or cacodylate buffer, pH 6.0, for the latter. Two-dimensional starch gel electrophoresis resolved at least 20 zones from the crotaline venom and 11 from the colubrid. Two zones of hemolytic activity were separated from each venom: in C. adamanteus the less cationic zone included possibly two or more acidic proteins; the corresponding zone of N. flava was more basic, more homogeneous, and more active under the conditions of assay.

STARCH GEL ELECTROPHORESIS OF COBRA AND RATTLESNAKE VENOMS

1963 ◽  
Vol 41 (4) ◽  
pp. 1073-1078 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Sodium Acetate ◽  
Acetate Buffer ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Acetate Buffer ◽  
Cacodylate Buffer ◽  
Starch Gel ◽  
Acidic Proteins

The effect of pH on gradient starch gel electrophoresis of the venoms of Crotalus adamanteus and Naja flava has been examined. Sodium acetate buffer, pH 4.1, ionic strength 0.020, appeared most effective for resolution of the former venom, and acetate buffer, pH 4.7, or cacodylate buffer, pH 6.0, for the latter. Two-dimensional starch gel electrophoresis resolved at least 20 zones from the crotaline venom and 11 from the colubrid. Two zones of hemolytic activity were separated from each venom: in C. adamanteus the less cationic zone included possibly two or more acidic proteins; the corresponding zone of N. flava was more basic, more homogeneous, and more active under the conditions of assay.

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.

ELECTROPHORESIS OF HISTONES ON POLYACRYLAMIDE GELS

1963 ◽  
Vol 41 (12) ◽  
pp. 2507-2516 ◽  
Author(s):  
A. Driedger ◽  
L. D. Johnson ◽  
A. M. Marko
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Polyacrylamide Gels ◽  
Optimum Conditions ◽  
Constant Ph ◽  
Starch Gel

Histories extracted from various organs of the rat have been fractionated by electrophoresis on Polyacrylamide gels. The most convenient reagents to form the gel were selected and the effects of varying concentrations of these reagents on the resolution of histones were investigated. Optimum conditions for the separation of histones were found to be the same as those for starch gel electrophoresis. More consistent results were obtained with the use of Polyacrylamide gels because these gels were equilibrated to constant pH and ionic strength prior to electrophoresis and the gels were electrophoretically destained to demonstrate the histone bands.

STUDIES ON PLASMINOGEN: IV. ALTERATION OF BOVINE AND HUMAN PLASMINOGENS DURING ISOLATION

1966 ◽  
Vol 44 (4) ◽  
pp. 469-473 ◽  
Author(s):  
John Y. S. Chan ◽  
Edwin T. Mertz
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Major Band ◽  
Starch Gel ◽  
Human Plasminogen

Bovine and human plasminogen preparations were analyzed by starch-gel electrophoresis at pH 2.5 and 0.10 ionic strength. The bands were activated with urokinase and the proteolytic and esterolytic activities measured. Bovine euglobulin contains one plasminogen band, B-1. Plasminogen prepared from bovine euglobulin by continuous electrophoresis at pH 3.5 contains B-1 and a faster plasminogen band, B-2. B-1 and B-2 are also found in bovine plasminogen prepared by DEAE-cellulose chromatography. All three preparations on activation give the same two plasmin bands on starch gel. Human euglobulin also contains two active plasminogen bands H-1 and H-2. Plasminogen prepared from human euglobulin by continuous electrophoresis at pH 3.5 contains H-1, H-2, and a faster minor plasminogen band, H-3. All highly purified human plasminogens derived from Cohn fraction III contain either H-3 as a major band and an additional plasminogen band, H-4, or only H-3, but no H-1 and H-2. On activation with urokinase or streptokinase, human plasminogen preparations give one or two plasmin bands. It is concluded that bovine B-2 and human H-3 and H-4 are altered forms of euglobulin plasminogen created during isolation procedures. Essentially pure human H-3 can be prepared by continuous electrophoresis from Cutter plasminogen.

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

1963 ◽  
Vol 41 (2) ◽  
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.

Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1317-1320 ◽  
Author(s):  
E. kaminski ◽  
W. Bushuk
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Direct Detection ◽  
Proteolytic Enzymes ◽  
Urea Concentration ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Multiple Forms ◽  
Starch Gel ◽  
Sensitive Method

A rapid and sensitive method for the direct detection of multiple forms of proteolytic enzymes by starch gel electrophoresis is described. The location of the enzyme components is identified by the degradation of hemoglobin which is included in the starch gel. This method was used to identify the enzyme components of the 10 commercial proteolytic enzymes bromelain, chymotrypsin, ficin, papain, pepsin, pronase B, protease, proteinase, and two preparations of trypsin. The effects of urea concentration and the ionic strength of aluminium lactate buffer were also examined. The best results were obtained with 3 M urea and with an ionic strength of 0.1 for the lactate buffer. It was observed that the number of enzyme components decreased with increasing concentrations of urea or increasing ionic strength of lactate buffer. The number of enzyme components did not always correspond to the number of protein bands. Self-digestion occurred in some of the protein bands in the starch gel after electrophoretic separation of the proteolytic enzymes.

A COMPARISON OF HISTONES FROM CHICKEN TISSUES BY ZONE ELECTROPHORESIS IN STARCH GEL

1961 ◽  
Vol 39 (3) ◽  
pp. 485-491 ◽  
Author(s):  
J. M. Neelin ◽  
G. C. Butler
Keyword(s):  
Cell Differentiation ◽  
Ionic Strength ◽  
Gel Electrophoresis ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Chicken Erythrocytes ◽  
Characteristic Zone

Histories were extracted at pH 1.7 from washed nuclei of chicken erythrocytes, spleen, liver, and testis and compared by starch-gel electrophoresis at pH 5.0, ionic strength 0.020. Spleen and liver histories displayed the most complex electrophoretic patterns with 18 zones each and differed only in relative proportions of certain zones. Erythrocyte histone contained a characteristic zone while lacking a group present in spleen and liver histones. Testis histone with only seven zones differed markedly from the other three. These results were consistent with chromatograms of erythrocyte, spleen, and liver histones on sodium IRC-50. The suggested correlation of tissue-specific histones with cell differentiation is discussed.

Muscle Proteins of the Coelacanth Latimeria Chalumnae Smith

1973 ◽  
Vol 53 (4) ◽  
pp. 763-784 ◽  
Author(s):  
G. Hamoir ◽  
A. Piront ◽  
Ch. Gerday ◽  
P. R. Dando
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
White Muscle ◽  
Protein Composition ◽  
Myofibrillar Proteins ◽  
Starch Gel Electrophoresis ◽  
High Concentration ◽  
Sarcoplasmic Proteins ◽  
Starch Gel ◽  
Muscle Types

Although the anatomy of the coelacanth muscles has been examined very thoroughly, their protein composition has, until recently, not been investigated. Thanks, however, to the 1972 British–French–American expedition to the Comores, frozen material has been made available and some results on myoglobin and four glycolytic enzymes have already been published. We have carried out a comparison of the sarcoplasmic proteins of red and white muscle by starch-gel electrophoresis. The ninhydrin-positive dialysable constituents and the myofibrillar proteins of white muscle have also been examined.A few puzzling results obtained with the white muscle extracts have been related to the occurrence of o.1 M ammonia, due presumably to the splitting of urea by a bacterial urease, and to an alteration of the active thiol groups of GAPDH and PK. If due account is taken of these unusual post-mortem changes, the extractability of the proteins and their properties are strikingly similar to those of teleosteans. The comparison of the sarcoplasmic proteins of white and red muscle by starch-gel electrophoresis revealed also that the differentiation observed in the coelacanth was similar to that occurring in the carp. A study of the low-molecular-weight proteins, or parvalbumins, of white muscle and of the myofibrillar proteins also shows the expected differences between the two muscle types.The only abnormal features observed in this study were the high concentration of parvalbumins, 1.5–2 times that found in other species examined, and the occurrence of an unusual globulin fraction which was easily extracted at ionic strength 0.5 and insoluble at ionic strength 0.35 and neutral pH.

FURTHER STUDIES OF CHANGES IN PLASMA PROTEINS IN AVIAN ERYTHROBLASTOSIS: I. TWO-DIMENSIONAL STARCH GEL ELECTROPHORESIS

1965 ◽  
Vol 43 (10) ◽  
pp. 1661-1665 ◽  
Author(s):  
Mohendra Merriman
Keyword(s):  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Starch Gel

Plasma protein changes in avian erythroblastosis previously studied with paper and starch gel electrophoresis have now been examined with a two-dimensional technique combining the two methods. The differences affect chiefly one zone which migrates in the α-globulin region.

SPECIES, TISSUE, AND INDIVIDUAL SPECIFICITY OF LOW IONIC STRENGTH EXTRACTS OF AVIAN MUSCLE AND OTHER ORGANS REVEALED BY STARCH-GEL ELECTROPHORESIS

1966 ◽  
Vol 44 (6) ◽  
pp. 853-859 ◽  
Author(s):  
C. M. Ann Baker
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Species Specificity ◽  
Major Protein ◽  
Starch Gel Electrophoresis ◽  
Avian Muscle ◽  
Starch Gel ◽  
Low Ionic Strength ◽  
Individual Specificity ◽  
Electrophoretic Resolution

The proteins soluble at low ionic strength of various muscles and of other tissues from five species of birds were examined by vertical starch-gel electrophoresis. The methods used were simple, and gave excellent and repeatable electrophoretic resolution of proteins. Most samples yielded 15–25 zones which stained nonspecifically for protein. Histochemical techniques revealed additional, enzyme, bands which were not coincident with the "major" protein zones. The results confirm and extend previous observations of the species specificity of the electrophoretic profiles of proteins from muscle extracts (myogen), and reveal considerable tissue and individual specificity of the enzymes and other proteins in extracts of avian tissues.

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